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Winnie-the-Pooh
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"Pooh" redirects here. For other uses, see Pooh (disambiguation).
"Hunny" redirects here. For the food, see Honey.
This article is about the fictional character. For the songwriter, see Poo Bear. For other uses, see Winnie-the-Pooh (disambiguation).
Winnie-the-Pooh
Pooh in an illustration by E. H. Shepard
First appearance
When We Were Very Young (1924) (As Edward Bear) Winnie-the-Pooh (As Winnie-the-Pooh)
Created by
A. A. Milne
Voiced by
Jim Cummings (1988-present) Sterling Holloway (1966-1977) Hal Smith (1981-1986) Franz Fazakas (1960)
Information
Nickname(s)
Pooh Bear
Pooh
Species
Bear
Gender
Male
Winnie-the-Pooh, also called Pooh Bear, is a fictional anthropomorphic teddy bear created by English author A. A. Milne.
The first collection of stories about the character was the book Winnie-the-Pooh (1926), and this was followed by The House at Pooh Corner (1928). Milne also included a poem about the bear in the children's verse book When We Were Very Young (1924) and many more in Now We Are Six (1927). All four volumes were illustrated by E. H. Shepard.
The Pooh stories have been translated into many languages, including Alexander Lenard's Latin translation, Winnie ille Pu, which was first published in 1958, and, in 1960, became the only Latin book ever to have been featured on The New York Times Best Seller list.[1]
Hyphens in the character's name were dropped by Disney when the company adapted the Pooh stories into a series of features that became one of its most successful franchises.
In popular film adaptations, Pooh Bear has been voiced by actors Sterling Holloway, Hal Smith, and Jim Cummings in English, and Yevgeny Leonov in Russian.
Contents
[hide]
1 History
1.1 Origin
1.2 Ashdown Forest: the setting for the stories
1.3 First publication
1.4 Character
1.5 Sequel
1.6 Stephen Slesinger
1.7 Red Shirt Pooh
1.8 Disney ownership era (1966–present)
1.9 Merchandising revenue dispute
2 Adaptations
2.1 Theatre
2.2 Audio
2.3 Radio
2.4 Film
2.4.1 Disney adaptations
2.4.1.1 Theatrical shorts
2.4.1.2 Theatrical feature films
2.4.2 Soviet adaptation
2.5 Television
2.5.1 Television shows
2.5.2 Holiday TV specials
2.5.3 Direct-to-video shorts
2.5.4 Direct-to-video features
2.5.5 Special TV appearances
3 Legacy
4 References
5 External links
History
Origin
Original Winnie-the-Pooh stuffed toys. Clockwise from bottom left: Tigger, Kanga, Edward Bear ("Winnie-the-Pooh"), Eeyore, and Piglet. Roo was lost long ago; the other characters were made up for the stories.
A. A. Milne named the character Winnie-the-Pooh after a teddy bear owned by his son, Christopher Robin Milne, who was the basis for the character Christopher Robin. The rest of Christopher Robin Milne's toys – Piglet, Eeyore, Kanga, Roo, and Tigger – were incorporated into Milne's stories.[2][3] Two more characters, Owl and Rabbit, were created by Milne's imagination, while Gopher was added to the Disney version. Christopher Robin's toy bear is on display at the Main Branch of the New York Public Library in New York City.[4]
Harry Colebourn and Winnie, 1914
Christopher Milne had named his toy bear after Winnie, a Canadian black bear he often saw at London Zoo, and "Pooh", a swan they had met while on holiday. The bear cub was purchased from a hunter for $20 by Canadian Lieutenant Harry Colebourn in White River, Ontario, Canada, while en route to England during the First World War.[5] He named the bear "Winnie" after his adopted hometown in Winnipeg, Manitoba. "Winnie" was surreptitiously brought to England with her owner, and gained unofficial recognition as The Fort Garry Horse regimental mascot. Colebourn left Winnie at the London Zoo while he and his unit were in France; after the war she was officially donated to the zoo, as she had become a much loved attraction there.[6] Pooh the swan appears as a character in its own right in When We Were Very Young.
Statue in Winnipeg of Harry Colebourn and Winnie
In the first chapter of Winnie-the-Pooh, Milne offers this explanation of why Winnie-the-Pooh is often called simply "Pooh":
But his arms were so stiff ... they stayed up straight in the air for more than a week, and whenever a fly came and settled on his nose he had to blow it off. And I think – but I am not sure – that that is why he is always called Pooh.
The American writer William Safire surmised that the Milnes' invention of the name "Winnie the Pooh" may have also been influenced by the haughty character Pooh-Bah in Gilbert and Sullivan's The Mikado (1885).[7]
Ashdown Forest: the setting for the stories
The Winnie-the-Pooh stories are set in Ashdown Forest, East Sussex, England. The forest is a large area of tranquil open heathland on the highest sandy ridges of the High Weald Area of Outstanding Natural Beauty situated 30 miles (50 km) south of London. In 1925 Milne, a Londoner, bought a country home a mile to the north of the forest at Cotchford Farm, near Hartfield. According to Christopher Milne, while his father continued to live in London "...the four of us – he, his wife, his son and his son's nanny – would pile into a large blue, chauffeur-driven Fiat and travel down every Saturday morning and back again every Monday afternoon. And we would spend a whole glorious month there in the spring and two months in the summer."[8] From the front lawn the family had a view across a meadow to a line of alders that fringed the River Medway, beyond which the ground rose through more trees until finally "above them, in the faraway distance, crowning the view, was a bare hilltop. In the centre of this hilltop was a clump of pines." Most of his father's visits to the forest at this time were, he noted, family expeditions on foot "to make yet another attempt to count the pine trees on Gill's Lap or to search for the marsh gentian". Christopher added that, inspired by Ashdown Forest, his father had made it "the setting for two of his books, finishing the second little over three years after his arrival".[9]
Many locations in the stories can be linked to real places in and around the forest. As Christopher Milne wrote in his autobiography: "Pooh’s forest and Ashdown Forest are identical". For example, the fictional "Hundred Acre Wood" was in reality Five Hundred Acre Wood; Galleon's Leap was inspired by the prominent hilltop of Gill's Lap, while a clump of trees just north of Gill's Lap became Christopher Robin's The Enchanted Place because no-one had ever been able to count whether there were sixty-three or sixty-four trees in the circle.[10]
The landscapes depicted in E. H. Shepard's illustrations for the Winnie-the-Pooh books were directly inspired by the distinctive landscape of Ashdown Forest, with its high, open heathlands of heather, gorse, bracken and silver birch punctuated by hilltop clumps of pine trees. Many of Shepard's illustrations can be matched to actual views, allowing for a degree of artistic licence. Shepard's sketches of pine trees and other forest scenes are held at the Victoria and Albert Museum in London.[11]
The game of Poohsticks was originally played by Christopher Milne on a footbridge across a tributary of the River Medway in Posingford Wood, close to Cotchford Farm. The wooden bridge is now a tourist attraction, and it has become traditional to play the game there using sticks gathered in nearby woodland.[12][13] When the footbridge recently had to be replaced, the engineer designed a new structure based closely on the drawings of the bridge by Shepard in the books, which were somewhat different than the original structure.
First publication
Winnie-the-Pooh's debut in the 24 December 1925 London Evening News
Christopher Robin's teddy bear, Edward, made his character début in A. A. Milne's poem, "Teddy Bear", in the edition of 13 February 1924 of Punch, and the same poem was published in Milne's book of children's verse When We Were Very Young (6 November 1924).[14] Winnie-the-Pooh first appeared by name on 24 December 1925, in a Christmas story commissioned and published by the London newspaper The Evening News. It was illustrated by J. H. Dowd.[15]
The first collection of Pooh stories appeared in the book Winnie-the-Pooh. The Evening News Christmas story reappeared as the first chapter of the book. At the beginning, it explained that Pooh was in fact Christopher Robin's Edward Bear, who had been renamed by the boy. He was renamed after a black bear at London Zoo called Winnie who got her name from the fact that her owner had come from Winnipeg, Canada. The book was published in October 1926 by the publisher of Milne's earlier children's work, Methuen, in England, and E. P. Dutton in the United States.[16]
Character
In the Milne books, Pooh is naive and slow-witted, but he is also friendly, thoughtful, and steadfast. Although he and his friends agree that he "has no Brain", Pooh is occasionally acknowledged to have a clever idea, usually driven by common sense. These include riding in Christopher Robin's umbrella to rescue Piglet from a flood, discovering "the North Pole" by picking it up to help fish Roo out of the river, inventing the game of Poohsticks, and getting Eeyore out of the river by dropping a large rock on one side of him to wash him towards the bank.
Pooh is also a talented poet, and the stories are frequently punctuated by his poems and "hums." Although he is humble about his slow-wittedness, he is comfortable with his creative gifts. When Owl's house blows down in a storm, trapping Pooh and Piglet and Owl inside, Pooh encourages Piglet (the only one small enough to do so) to escape and rescue them all by promising that "a respectful Pooh song" will be written about Piglet's feat. Later, Pooh muses about the creative process as he composes the song.
Pooh is very fond of food, especially "hunny" but also condensed milk and other items. When he visits friends, his desire to be offered a snack is in conflict with the impoliteness of asking too directly. Though intending to give Eeyore a pot of honey for his birthday, Pooh cannot resist eating the honey on his way to deliver the present, and so instead gives Eeyore "a useful pot to put things in". When he and Piglet are lost in the forest during Rabbit's attempt to "unbounce" Tigger, Pooh finds his way home by following the "call" of the honeypots from his house. Pooh makes it a habit to have "a little something" around eleven o'clock in the morning. As the clock in his house "stopped at five minutes to eleven some weeks ago," any time can be Pooh's snack time.
Pooh is very social. After Christopher Robin, his closest friend is Piglet, and he most often chooses to spend his time with one or both of them. But he also habitually visits the other animals, often looking for a snack or an audience for his poetry as much as for companionship. His kind-heartedness means he goes out of his way to be friendly to Eeyore, visiting him and bringing him a birthday present and building him a house, despite receiving mostly disdain from Eeyore in return.
Sequel
An authorised sequel Return to the Hundred Acre Wood was published on 5 October 2009. The author, David Benedictus, has developed, but not changed, Milne's characterisations. The illustrations, by Mark Burgess, are in the style of Shepard.[17]
Another authorised sequel, The Best Bear in All the World, was published by Egmont in 2016. The sequel consists of four short stories by four leading children's authors, Kate Saunders, Brian Sibley, Paul Bright, and Jeanne Willis. Illustrations are by Mark Burgess.[18] The Best Bear in All The World sees the introduction of a new character, a Penguin, which was inspired by a long-lost photograph of Milne and his son Christopher with a toy penguin.[19] A further special story, Winnie-the-Pooh Meets the Queen, was published in 2016 to mark the 90th anniversary of Milne's creation and the 90th birthday of Elizabeth II. It sees Winnie the Pooh meet the Queen at Buckingham Palace.[20]
Stephen Slesinger
On 6 January 1930, Stephen Slesinger purchased US and Canadian merchandising, television, recording and other trade rights to the "Winnie-the-Pooh" works from Milne for a $1000 advance and 66% of Slesinger's income, creating the modern licensing industry. By November 1931, Pooh was a $50 million-a-year business.[21] Slesinger marketed Pooh and his friends for more than 30 years, creating the first Pooh doll, record, board game, puzzle, US radio broadcast (NBC), animation, and motion picture film.[22]
Red Shirt Pooh
The first time Pooh and his friends appeared in colour was 1932, when he was drawn by Slesinger in his now-familiar red shirt and featured on an RCA Victor picture record. Parker Brothers introduced A. A. Milne's Winnie-the-Pooh Game in 1933, again with Pooh in his red shirt. In the 1940s, Agnes Brush created the first plush dolls with Pooh in his red shirt. Shepard had drawn Pooh with a shirt as early as the first Winnie-The-Pooh book, which was subsequently coloured red in later coloured editions.
Disney ownership era (1966–present)
Main article: Winnie the Pooh (franchise)
After Slesinger's death in 1953, his wife, Shirley Slesinger Lasswell, continued developing the character herself. In 1961, she licensed rights to Walt Disney Productions in exchange for royalties in the first of two agreements between Stephen Slesinger, Inc. and Disney.[23] The same year, A. A. Milne's widow, Daphne Milne, also licensed certain rights, including motion picture rights, to Disney.
Since 1966, Disney has released numerous animated productions starring Winnie the Pooh and related characters. These have included theatrical featurettes, television series, and direct-to-video films, as well as the theatrical feature-length films The Tigger Movie, Piglet's Big Movie, Pooh's Heffalump Movie, and Winnie the Pooh.
Merchandising revenue dispute
Pooh videos, soft toys, and other merchandise generate substantial annual revenues for Disney. The size of Pooh stuffed toys ranges from Beanie and miniature to human-sized. In addition to the stylised Disney Pooh, Disney markets Classic Pooh merchandise which more closely resembles E.H. Shepard's illustrations.
In 1991, Stephen Slesinger, Inc. filed a lawsuit against Disney which alleged that Disney had breached their 1983 agreement by again failing to accurately report revenue from Winnie the Pooh sales. Under this agreement, Disney was to retain approximately 98% of gross worldwide revenues while the remaining 2% was to be paid to Slesinger. In addition, the suit alleged that Disney had failed to pay required royalties on all commercial exploitation of the product name.[24] Though the Disney corporation was sanctioned by a judge for destroying forty boxes of evidential documents,[25] the suit was later terminated by another judge when it was discovered that Slesinger's investigator had rummaged through Disney's garbage to retrieve the discarded evidence.[26] Slesinger appealed the termination and, on 26 September 2007, a three-judge panel upheld the lawsuit dismissal.[27]
After the Copyright Term Extension Act of 1998, Clare Milne, Christopher Milne's daughter, attempted to terminate any future US copyrights for Stephen Slesinger, Inc.[28] After a series of legal hearings, Judge Florence-Marie Cooper of the US District Court in California found in favour of Stephen Slesinger, Inc., as did the United States Court of Appeals for the Ninth Circuit. On 26 June 2006, the US Supreme Court refused to hear the case, sustaining the ruling and ensuring the defeat of the suit.[29]
On 19 February 2007 Disney lost a court case in Los Angeles which ruled their "misguided claims" to dispute the licensing agreements with Slesinger, Inc. were unjustified,[30] but a federal ruling of 28 September 2009, again from Judge Florence-Marie Cooper, determined that the Slesinger family had granted all trademarks and copyrights to Disney, although Disney must pay royalties for all future use of the characters. Both parties have expressed satisfaction with the outcome.[31][32]
Adaptations
Theatre
Winnie-the-Pooh at the Guild Theater, Sue Hastings Marionettes, 1931[33]
Winnie-the-Pooh, a play in three acts, dramatized by Kristin Sergel, Dramatic Publishing Company, 1957
Winnie-the-Pooh, a musical comedy in two acts, lyrics by A. A. Milne and Kristin Sergel, music by Allan Jay Friedman, book by Kristin Sergel, Dramatic Publishing Company, 1964
A Winnie-the-Pooh Christmas Tail, In Which Winnie-the-Pooh and His Friends Help Eeyore Have a Very Merry Christmas (Or a Very Happy Birthday.), book, music, and lyrics by James W. Rogers, Dramatic Publishing Company, 1977
"Bother! The Brain of Pooh", Peter Dennis, 1986
Winnie-the-Pooh, small cast musical version, dramatized by le Clanché du Rand, music by Allan Jay Friedman, lyrics by A. A. Milne and Kristin Sergel, additional lyrics by le Clanché du Rand, Dramatic Publishing Company, 1992
Audio
RCA Victor record from 1932 decorated with Stephen Slesinger, Inc.'s Winnie-the-Pooh
Selected Pooh stories read by Maurice Evans released on vinyl LP:
Winnie-the-Pooh (consisting of three tracks: "Introducing Winnie-the-Pooh and Christopher Robin"; Pooh Goes Visiting and Gets into a Tight Place"; "Pooh and Piglet Go Hunting and Nearly Catch a Woozle") 1956
More Winnie-the-Pooh (consisting of three tracks: "Eeyore Loses a Tail"; "Piglet Meets a Heffalump"; "Eeyore Has a Birthday".)
In 1960 HMV recorded a dramatised version with songs (music by Harold Fraser-Simson) of two episodes from The House at Pooh Corner (Chapters 2 and 8), starring Ian Carmichael as Pooh, Denise Bryer as Christopher Robin (who also narrated), Hugh Lloyd as Tigger, Penny Morrell as Piglet, and Terry Norris as Eeyore. This was released on a 45 rpm EP.[34]
In the 1970s and 1980s, Carol Channing recorded Winnie the Pooh, The House at Pooh Corner and The Winnie the Pooh Songbook, with music by Don Heckman. These were released on vinyl LP and audio cassette by Caedmon Records.
Unabridged recordings read by Peter Dennis of the four Pooh books:
When We Were Very Young
Winnie-the-Pooh
Now We Are Six
The House at Pooh Corner
In 1979 a double audio cassette set of "Winnie the Pooh" was produced featuring British actor Lionel Jeffries reading all characters in the stories. This was followed in 1981 by an audio cassette set of stories from "House at Pooh Corner" also read by Lionel Jeffries.[35]
In the 1990s, the stories were dramatised for audio by David Benedictus, with music composed, directed and played by John Gould. They were performed by a cast that included Stephen Fry as Winnie-the-Pooh, Jane Horrocks as Piglet, Geoffrey Palmer as Eeyore, and Judi Dench as Kanga.[36]
Radio
Winnie-the-Pooh was broadcast by Donald Calthrop over all BBC stations on Christmas Day, 1925.[15]
Pooh made his US radio debut on 10 November 1932, when he was broadcast to 40,000 schools by The American School of the Air, the educational division of the Columbia Broadcasting System.[37]
Film
2017: Goodbye Christopher Robin, a drama film exploring the creation of Winnie-the-Pooh by A.A. Milne.
Disney adaptations
Theatrical shorts
1966: Winnie the Pooh and the Honey Tree
1968: Winnie the Pooh and the Blustery Day
1974: Winnie the Pooh and Tigger Too
1981: Winnie the Pooh Discovers the Seasons
1983: Winnie the Pooh and a Day for Eeyore
Theatrical feature films
1977: The Many Adventures of Winnie the Pooh (compilation of Honey Tree, Blustery Day, and Tigger Too)
2000: The Tigger Movie
2003: Piglet's Big Movie
2005: Pooh's Heffalump Movie
2011: Winnie the Pooh
2018: Christopher Robin[38][39]
Soviet adaptation
A postage stamp showing Piglet and Winnie-the-Pooh as they appear in the Soviet adaptation
In the Soviet Union, three Winnie-the-Pooh, (transcribed in Russian as "Vinni Pukh") (Russian language: Винни-Пух) stories were made into a celebrated trilogy[40] of short films by Soyuzmultfilm (directed by Fyodor Khitruk) from 1969 to 1972.
Винни-Пух (Winnie-the-Pooh, 1969) – based on chapter 1
Винни-Пух идёт в гости (Winnie-the-Pooh Pays a Visit, 1971) – based on chapter 2
Винни-Пух и день забот (Winnie the Pooh and the Blustery Day, 1972) – based on chapters 4 and 6.
Films use Boris Zakhoder's translation of the book. Pooh was voiced by Yevgeny Leonov. Unlike the Disney adaptations, the animators did not base their depictions of the characters on Shepard's illustrations, creating a different look. The Soviet adaptations make extensive use of Milne's original text, and often bring out aspects of Milne's characters' personalities not used in the Disney adaptations.
Television
Winnie-the-Pooh and his friends debuted on NBC Television in 1960.
A version of Winnie The Pooh, in which the animals were played by marionettes designed, made and operated by Bil And Cora Baird, was presented on 3 October 1960, on NBC Television's The Shirley Temple Show. Pooh himself is voiced by Franz Fazakas.
During the 1970s the BBC children's television show Jackanory serialised the two books, which were read by Willie Rushton.[41]
Magical World of Winnie the Pooh (Note: These are episodes from The New Adventures of Winnie the Pooh)
Television shows
Welcome to Pooh Corner (*) (Disney Channel, 1983–1986)
Mini Adventures of Winnie the Pooh (Disney Junior, 2011–2014[42])
The New Adventures of Winnie the Pooh (ABC, 1988–1991)
The Book of Pooh (*) (Disney Channel (Playhouse Disney), 2001–2003)
My Friends Tigger & Pooh (Disney Channel (Playhouse Disney), 2007–2010)
(*): Puppet/live-action show
Holiday TV specials
1991: Winnie the Pooh and Christmas Too, included in A Very Merry Pooh Year
1996: Boo to You Too! Winnie the Pooh, included in Pooh's Heffalump Halloween Movie
1998: A Winnie the Pooh Thanksgiving, included in Seasons of Giving
1999: A Valentine for You
Direct-to-video shorts
1990: Winnie the Pooh's ABC of Me
Direct-to-video features
1997: Pooh's Grand Adventure: The Search for Christopher Robin
1999: Seasons of Giving*
2001: The Book of Pooh: Stories from the Heart
2002: A Very Merry Pooh Year*
2004: Springtime with Roo
2005: Pooh's Heffalump Halloween Movie
2007: Super Sleuth Christmas Movie
2009: Tigger & Pooh and a Musical Too
2010: Super Duper Super Sleuths
These features integrate stories from The New Adventures of Winnie the Pooh and/or holiday specials with new footage.
Special TV appearances
1958: Shirley Temple's Storybook: Winnie-the-Pooh
Legacy
A plaque on Winnie-the-Pooh Street (ulica Kubusia Puchatka) in Warsaw
Winnie the Pooh has inspired multiple texts to explain complex philosophical ideas. Benjamin Hoff used Milne's characters in The Tao of Pooh and The Te of Piglet to explain Taoism. Similarly, Frederick Crews wrote essays about the Pooh books in abstruse academic jargon in The Pooh Perplex and Postmodern Pooh to satirise a range of philosophical approaches.[43] Pooh and the Philosophers by John T. Williams uses Winnie the Pooh as a backdrop to illustrate the works of philosophers including Descartes, Kant, Plato, and Nietzsche.[44]
One of the best known characters in British children's literature, a 2011 poll saw Winnie the Pooh voted onto the list of icons of England.[45] Forbes magazine ranked Pooh the most valuable fictional character in 2002, with merchandising products alone generating more than $5.9 billion that year.[46] In 2005, Pooh generated $6 billion, a figure surpassed by only Mickey Mouse.[47] In 2006, Pooh received a star on the Hollywood Walk of Fame, marking the 80th birthday of Milne's creation.[47] The bear is such a popular character in Poland that a Warsaw street is named for him, Ulica Kubusia Puchatka. There is also a street named after him in Budapest (Micimackó utca).[48]
In music, Kenny Loggins wrote the song "House at Pooh Corner", which was originally recorded by the Nitty Gritty Dirt Band.[49] Loggins later rewrote the song as "Return to Pooh Corner", featuring on the album of the same name in 1991. In Italy, a pop band took their name from Winnie, and were titled Pooh. In Estonia there is a punk/metal band called Winny Puhh.
In the "sport" of Poohsticks, competitors drop sticks into a stream from a bridge and then wait to see whose stick will cross the finish line first. Though it began as a game played by Pooh and his friends in the book The House at Pooh Corner and later in the films, it has crossed over into the real world: a World Championship Poohsticks race takes place in Oxfordshire each year. Ashdown Forest in England where the Pooh stories are set is a popular tourist attraction, and includes the wooden Pooh Bridge where Pooh and Piglet invented Poohsticks.[50] The Oxford University Winnie the Pooh Society was founded by undergraduates in 1982.
In the Peoples Republic of China, images of Pooh were censored in mid-2017 from social media websites, when internet memes comparing Chinese president Xi Jinping to Pooh became popular.[51]
References
Jump up ^ McDowell, Edwin. "Winnie Ille Pu Nearly XXV Years Later", The New York Times (18 November 1984). Retrieved 2 January 2010.
Jump up ^ "Pooh celebrates his 80th birthday". BBC News. Retrieved 20 July 2015
Jump up ^ Ford, Rebecca (28 February 2007) "Happy Birthday Pooh", Daily Express. Retrieved 20 July 2015
Jump up ^ "The Adventures of the Real Winnie-the-Pooh. The New York Public Library.
Jump up ^ "Winnie the Pooh's Canadian beginnings". The Spectator, – Hamilton, Ont. 2 August 1997, Page: W.13
Jump up ^ "Winnie". Historica Minutes, The Historica Foundation of Canada. Retrieved 30 May 2008.
Jump up ^ Safire, William. “Whence Poo-Bah”, GASBAG, vol. 24, no. 3, issue 186, January/February 1993, p. 28.
Jump up ^ Willard, Barbara (1989). The Forest – Ashdown in East Sussex. Sussex: Sweethaws Press. . Quoted from the Introduction, p. xi, by Christopher Milne.
Jump up ^ Willard (1989). Quoted from the Introduction, p. xi, by Christopher Milne.
Jump up ^ Hope, Yvonne Jefferey (2000). "Winnie-the-Pooh in Ashdown Forest". In Brooks, Victoria. Literary Trips: Following in the Footsteps of Fame. 1. Vancouver, Canada: Greatest Escapes. p. 287. ISBN 0-9686137-0-5.
Jump up ^ "About the E. H. Shepard archive". University of Surrey. Retrieved 1 May 2012.
Jump up ^ "Plans to improve access to Pooh Bridge unveiled". BBC News. Retrieved 11 November 2012
Jump up ^ "Appeal to save Winnie the Pooh's bridge". BBC News. Retrieved 11 November 2012
Jump up ^ "Celebrate Winnie-The-Pooh's 90th with a Rare Recording (And Hunny)". NPR. 20 July 2015.
^ Jump up to: a b "A Children's Story by A. A. Milne". London Evening News. 24 December 1925. p. 1.
Jump up ^ Thwaite, Ann (2004). Oxford Dictionary of National Biography: Alan Alexander Milne. Oxford: Oxford University Press.
Jump up ^ Kennedy, Maev (4 October 2009). "Pooh sequel returns Christopher Robin to Hundred Acre Wood". The Guardian. UK. p. 15. |access-date= requires |url= (help)
Jump up ^ "Winnie-the-Pooh sequel details revealed". Retrieved 18 October 2016.
Jump up ^ "Listen to the moment Winnie-the-Pooh meets penguin friend in new book". BBC News. 19 September 2016.
Jump up ^ "Winnie the Pooh meets the Queen in a new story". BBC News. 19 September 2016.
Jump up ^ "The Merchant of Child". Fortune. November 1931. p. 71.
Jump up ^ McElway, St. Claire (26 October 1936). "The Literary Character in Business & Commerce". The New Yorker.
Jump up ^ "The Curse of Pooh." Fortune.
Jump up ^ "The Pooh Files" The Albion Monitor.
Jump up ^ Nelson, Valerie J (20 July 2007). "Shirley Slesinger Lasswell, 84; fought Disney over Pooh royalties". Los Angeles Times. Retrieved 14 August 2007. [dead link]
Jump up ^ "Judge dismisses Winnie the Pooh lawsuit" The Disney Corner.
Jump up ^ James, Meg (26 September 2007). "Disney wins lawsuit ruling on Pooh rights". Los Angeles Times. Retrieved 26 September 2007. [dead link]
Jump up ^ "Winnie the Pooh goes to court" USA Today
Jump up ^ "USATODAY.com – Justices won't hear copyright appeal by relative of Winnie the Pooh". USA Today. Associated Press.
Jump up ^ "Disney loses court battle in Winnie the Pooh copyright case". ABC News. 17 February 2007. Retrieved 15 May 2008.
Jump up ^ James, Meg (29 September 2009). "Pooh rights belong to Disney, judge rules". Los Angeles Times. Retrieved 5 October 2009.
Jump up ^ Shea, Joe (4 October 2009). "The gordian knot of Pooh rights is finally untied in federal court". The American Reporter. Retrieved 5 October 2009. [dead link]
Jump up ^ "Hastings Marionettes: Will Open Holiday Season at Guild Theatre on Saturday". The New York Times. 22 December 1931. p. 28.
Jump up ^ "Ian Carmichael And Full Cast – The House at Pooh Corner – HMV Junior Record Club – UK – 7EG 117". 45cat. 23 July 2010. Retrieved 5 November 2011.
Jump up ^ "Winnie the Pooh". OCLC WorldCat. Retrieved 15 January 2016.
Jump up ^ "Tigger comes to the forest: and other stories". OCLC WorldCat. Retrieved 15 January 2016.
Jump up ^ "His Master's Voice Speaks Again". Playthings. November 1932.
Jump up ^ Fleming Jr., Mike. "Disney Sets Live-Action 'Winnie The Pooh' Film; Alex Ross Perry To Write". Deadline. Retrieved 6 April 2015.
Jump up ^ Lincoln, Ross A. (18 November 2016). "Marc Forster To Helm Live-Action 'Christopher Robin' Based On 'Winnie The Pooh' Character". Deadline.
Jump up ^ "Russian animation in letters and figures | "Winnie the Pooh"". Animator.ru. Retrieved 9 March 2015.
Jump up ^ Biography: Willie Rushton. BBC. Retrieved 11 March 2015.
Jump up ^ "Mini Adventures of Winnie the Pooh". IMDb. 22 August 2011. Retrieved 15 January 2016.
Jump up ^ spiked-culture |Article |Pooh-poohing postmodernism. Spiked-online.com. Retrieved 12 February 2011.
Jump up ^ Sonderbooks Book Review of Pooh and the Philosophers. Sonderbooks.com (20 April 2004). Retrieved 12 February 2011.
Jump up ^ "ICONS of England – the 100 ICONS as voted by the public". Culture 24 News. 20 July 2015.
Jump up ^ "Top-Earning Fictional Characters". Forbes (New York). 25 September 2003. Retrieved 11 November 2012.
^ Jump up to: a b "Pooh joins Hollywood Walk of Fame". BBC. Retrieved 24 November 2014
Jump up ^ "Google Maps". Google Maps. 1 January 1970. Retrieved 9 March 2015.
Jump up ^ "House at Pooh Corner by Loggins and Messina Songfacts". Songfacts.com. 14 October 1926. Retrieved 9 March 2015.
Jump up ^ Plans to improve access to Pooh Bridge unveiled. BBC. Retrieved 15 October 2011
Jump up ^ McDonell, Stephen (17 July 2017). "Why China censors banned Winnie the Pooh". BBC News. Retrieved 6 October 2017.
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Winnie-the-Pooh at Curlie (based on DMOZ)
The original bear, with A. A. Milne and Christopher Robin, at the National Portrait Gallery, London
The real locations, from the Ashdown Forest Conservators
Winnie-the-Pooh at the New York Public Library
"Winnie the Pooh saga turns 100 years old", CBC News, 24 August 2014.
"The skull of the 'real' Winnie goes on display", BBC News, 20 November 2015.
[show]
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Winnie-the-Pooh by A. A. Milne
Books
When We Were Very Young (1924)
Winnie-the-Pooh (1926)
Now We Are Six (1927)
The House at Pooh Corner (1928)
Return to the Hundred Acre Wood (2009)
The Best Bear in All the World (2016)
Winnie-the-Pooh Meets the Queen (2016)
Characters
Winnie-the-Pooh
Disney version
Piglet
Tigger
Christopher Robin
Rabbit
Eeyore
Owl
Roo
Heffalumps
Gopher
Featurettes
Winnie the Pooh and the Honey Tree (1966)
Winnie the Pooh and the Blustery Day (1968)
Winnie-the-Pooh (1969)
Winnie-the-Pooh Pays a Visit (1971)
Winnie-the-Pooh and a Busy Day (1972)
Winnie the Pooh and Tigger Too (1974)
Winnie the Pooh and a Day for Eeyore (1983)
Short films
Winnie the Pooh Discovers the Seasons (1981)
Feature films
Walt Disney Animation Studios films
The Many Adventures of Winnie the Pooh (1977)
Winnie the Pooh (2011)
DisneyToon Studios films
The Tigger Movie (2000)
Piglet's Big Movie (2003)
Pooh's Heffalump Movie (2005)
Live-action remake
Christopher Robin (2018)
Direct-to-video films
Pooh's Grand Adventure: The Search for Christopher Robin (1997)
Winnie the Pooh: Seasons of Giving (1999)
The Book of Pooh: Stories from the Heart (2001)
Winnie the Pooh: A Very Merry Pooh Year (2002)
Winnie the Pooh: Springtime with Roo (2004)
Pooh's Heffalump Halloween Movie (2005)
Super Sleuth Christmas Movie (2007)
Tigger & Pooh and a Musical Too (2009)
Super Duper Super Sleuths (2010)
Television
Welcome to Pooh Corner (1983–1987)
The New Adventures of Winnie the Pooh (1988–1991)
The Book of Pooh (2001–2004)
My Friends Tigger & Pooh (2007–2010)
Specials
Cartoon All-Stars to the Rescue (1990)
Winnie the Pooh and Christmas Too (1991)
Boo to You Too! Winnie the Pooh (1996)
A Winnie the Pooh Thanksgiving (1998)
A Valentine for You (1999)
Video games
Winnie the Pooh in the Hundred Acre Wood (1986)
Disney's Animated Storybook
Winnie the Pooh and the Honey Tree (1995)
Winnie the Pooh and Tigger Too (1999)
Kingdom Hearts (2002 onwards
Ready to Read with Pooh (1997)
Tigger's Honey Hunt (2000)
Piglet's Big Game (2003)
Winnie the Pooh's Rumbly Tumbly Adventure (2005)
Disney Friends (2007)
Winnie the Pooh's Home Run Derby (2007)
Songs
"Winnie the Pooh" (1966)
"Up, Down and Touch the Ground" (1966)
"Rumbly in My Tumbly" (1966)
"Little Black Rain Cloud" (1966)
"Mind over Matter" (1966)
"A Rather Blustery Day" (1968)
"The Wonderful Thing About Tiggers" (1968)
"Heffalumps and Woozles" (1968)
"The Rain Rain Rain Came Down Down Down" (1968)
"Hip Hip Pooh-Ray!" (1968)
"House at Pooh Corner" (1970)
"I Hum to Myself" (1983)
"The Right Side" (1983)
"You're the Only You" (1983)
"Try a Little Something New" (1983)
People
Christopher Robin Milne
E. H. Shepard
Harry Colebourn
Shirley Slesinger Lasswell
Stephen Slesinger
Sherman Brothers
David Benedictus
Mark Burgess
Related
Ashdown Forest
Bother! The Brain of Pooh
Disney franchise
Hundred Acre Wood
The Many Adventures of Winnie the Pooh attraction
More Songs from Pooh Corner
Pooh's Hunny Hunt
Poohsticks
Return to Pooh Corner
The Tao of Pooh
The Te of Piglet
Eeyore's Birthday Party
Winnipeg the Bear
A Bear Named Winnie
Goodbye Christopher Robin
[show]
v
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Teddy bears
Manufacturers
Build-A-Bear Workshop
Chad Valley
J. K. Farnell
Gund
Ideal Toy Company
Margarete Steiff GmbH
Merrythought
Teddy Atelier Stursberg
Teddy-Hermann
Ty Inc.
Vermont Teddy Bear Company
Types
AG Bear
Beanie Babies
Boyds Bears
Care Bears
Coffee Bean Bears
Forever Friends
Freddy Teddy
Gund Snuffles
Holiday Beanie Babies
Me to You Bears
WereBears
Museums
Dorset Teddy Bear Museum
Teddy bear museum
Teddy Bear Museum of Naples
Famous teddies
Aloysius
Archibald Ormsby-Gore
Benjamin Bear
Bamse
Berlino
Duffy the Disney Bear
Corduroy
Fozzie Bear
Freddy Fazbear
Grizzly Teddy
Lotso
Microsoft Bear
Misha
Nassur
Nev
Paddington Bear
Pooky
Pudsey Bear
Rilakkuma
Roosevelt
Rupert Bear
Rupert (Family Guy)
Smokey
Sooty
SuperTed
Teddy (Mr. Bean)
Teddy Ruxpin
Uszatek
Mr Whoppit
Winnie-the-Pooh
Yogi Bear
Film and television
The Adventures of Teddy Ruxpin
Bear Behaving Badly
Becky and Barnaby Bear
Boonie Bears
C Bear and Jamal
Colargol
Disney's Adventures of the Gummi Bears
Issi Noho
Old Bear Stories
Paddington
The Secret World of Benjamin Bear
SuperTed
Ted
Ted 2
Teddybears
The Teddy Bear Master
Teddy Edward
The Upstairs Downstairs Bears
The Yogi Bear Show
Books
Corduroy
Little Bear
Old Bear and Friends
Teddy Dressing
The Berenstain Bears
Polar the Titanic Bear
Uppo-Nalle
Winkie
Winnie-the-Pooh
Music
"(Let Me Be Your) Teddy Bear"
"Psycho Teddy"
"Teddy Bears' Picnic"
"The Teddy Bear Song"
Video games
Build-A-Bear Workshop
Hubert the Teddy Bear: Winter Games
Opération Teddy Bear
Teddy Together
Related topics
The Bear Club
Peter Bull
Gummy bears
Round and Round the Garden
SGUL Teddy Bear Hospital
Richard Steiff
Stuffed toys
Sudanese blasphemy case
Teddybear Airdrop Minsk 2012
Teddy bear parachuting
Teddy Bear Review
Teddy bear toss
Teddy Grahams
Authority control
WorldCat Identities
VIAF: 33185902
LCCN: no2014169001
GND: 133372065
NLA: 58458776
United Kingdom portal
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Disney portal
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text:
Electron transport chain
From Wikipedia, the free encyclopedia
Jump to: navigation, search
The electron transport chain in the mitochondrion is the site of oxidative phosphorylation in eukaryotes. The NADH and succinate generated in the citric acid cycle are oxidized, providing energy to power ATP synthase.
Photosynthetic electron transport chain of the thylakoid membrane.
An electron transport chain (ETC) is a series of complexes that transfer electrons from electron donors to electron acceptors via redox (both reduction and oxidation occurring simultaneously) reactions, and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. This creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP), a molecule that stores energy chemically in the form of highly strained bonds. The molecules of the chain include peptides, enzymes (which are proteins or protein complexes), and others. The final acceptor of electrons in the electron transport chain during aerobic respiration is molecular oxygen although a variety of acceptors other than oxygen such as sulfate exist in anaerobic respiration.
Electron transport chains are used for extracting energy via redox reactions from sunlight in photosynthesis or, such as in the case of the oxidation of sugars, cellular respiration. In eukaryotes, an important electron transport chain is found in the inner mitochondrial membrane where it serves as the site of oxidative phosphorylation through the use of ATP synthase. It is also found in the thylakoid membrane of the chloroplast in photosynthetic eukaryotes. In bacteria, the electron transport chain is located in their cell membrane.
In chloroplasts, light drives the conversion of water to oxygen and NADP+ to NADPH with transfer of H+ ions across chloroplast membranes. In mitochondria, it is the conversion of oxygen to water, NADH to NAD+ and succinate to fumarate that are required to generate the proton gradient.
Electron transport chains are major sites of premature electron leakage to oxygen, generating superoxide and potentially resulting in increased oxidative stress.
Contents
[hide]
1 Background
2 In mitochondria
2.1 Mitochondrial redox carriers
2.1.1 Complex I
2.1.2 Complex II
2.1.3 Complex III
2.1.4 Complex IV
2.2 Coupling with oxidative phosphorylation
2.3 Summary
3 In bacteria
3.1 Electron donors
3.2 Dehydrogenases
3.3 Quinone carriers
3.4 Proton pumps
3.5 Cytochrome electron carriers
3.6 Terminal oxidases and reductases
3.7 Electron acceptors
3.8 Summary
4 Photosynthetic
5 Summary
6 See also
7 References
8 External links
Background[edit]
The electron transport chain consists of a spatially separated series of redox reactions in which electrons are transferred from a donor molecule to an acceptor molecule. The underlying force driving these reactions is the Gibbs free energy of the reactants and products. The Gibbs free energy is the energy available ("free") to do work. Any reaction that decreases the overall Gibbs free energy of a system is thermodynamically spontaneous.
The function of the electron transport chain is to produce a transmembrane proton electrochemical gradient as a result of the redox reactions.[1] If protons flow back through the membrane, they enable mechanical work, such as rotating bacterial flagella. ATP synthase, an enzyme highly conserved among all domains of life, converts this mechanical work into chemical energy by producing ATP,[2] which powers most cellular reactions. A small amount of ATP is available from substrate-level phosphorylation, for example, in glycolysis. In most organisms the majority of ATP is generated in electron transport chains, while only some obtain ATP by fermentation.[citation needed]
In mitochondria[edit]
Most eukaryotic cells have mitochondria, which produce ATP from products of the citric acid cycle, fatty acid oxidation, and amino acid oxidation. At the mitochondrial inner membrane, electrons from NADH and FADH2 pass through the electron transport chain to oxygen, which is reduced to water. The electron transport chain comprises an enzymatic series of electron donors and acceptors. Each electron donor will pass electrons to a more electronegative acceptor, which in turn donates these electrons to another acceptor, a process that continues down the series until electrons are passed to oxygen, the most electronegative and terminal electron acceptor in the chain. Passage of electrons between donor and acceptor releases energy, which is used to generate a proton gradient across the mitochondrial membrane by actively "pumping" protons into the intermembrane space, producing a thermodynamic state that has the potential to do work. The entire process is called oxidative phosphorylation, since ADP is phosphorylated to ATP using the energy of hydrogen oxidation in many steps.
A small percentage of electrons do not complete the whole series and instead directly leak to oxygen, resulting in the formation of the free-radical superoxide, a highly reactive molecule that contributes to oxidative stress and has been implicated in a number of diseases and aging.
Mitochondrial redox carriers[edit]
Energy obtained through the transfer of electrons down the ETC is used to pump protons from the mitochondrial matrix into the intermembrane space, creating an electrochemical proton gradient (ΔpH) across the inner mitochondrial membrane (IMM). This proton gradient is largely but not exclusively responsible for the mitochondrial membrane potential (ΔΨM). It allows ATP synthase to use the flow of H+ through the enzyme back into the matrix to generate ATP from adenosine diphosphate (ADP) and inorganic phosphate. Complex I (NADH coenzyme Q reductase; labeled I) accepts electrons from the Krebs cycle electron carrier nicotinamide adenine dinucleotide (NADH), and passes them to coenzyme Q (ubiquinone; labeled Q), which also receives electrons from complex II (succinate dehydrogenase; labeled II). Q passes electrons to complex III (cytochrome bc1 complex; labeled III), which passes them to cytochrome c (cyt c). Cyt c passes electrons to Complex IV (cytochrome c oxidase; labeled IV), which uses the electrons and hydrogen ions to reduce molecular oxygen to water.
Four membrane-bound complexes have been identified in mitochondria. Each is an extremely complex transmembrane structure that is embedded in the inner membrane. Three of them are proton pumps. The structures are electrically connected by lipid-soluble electron carriers and water-soluble electron carriers. The overall electron transport chain:
NADH+H+ → Complex I → Q → Complex III → cytochrome c → Complex IV → H2O ↑ Complex II ↑ Succinate

Complex I[edit]
In Complex I (NADH:ubiquinone oxidoreductase, NADH-CoQ reductase, or NADH dehydrogenase; EC 1.6.5.3), two electrons are removed from NADH and ultimately transferred to a lipid-soluble carrier, ubiquinone (UQ). The reduced product, ubiquinol (UQH2), freely diffuses within the membrane, and Complex I translocates four protons (H+) across the membrane, thus producing a proton gradient. Complex I is one of the main sites at which premature electron leakage to oxygen occurs, thus being one of the main sites of production of superoxide.[3]
The pathway of electrons is as follows:
NADH is oxidized to NAD+, by reducing Flavin mononucleotide to FMNH2 in one two-electron step. FMNH2 is then oxidized in two one-electron steps, through a semiquinone intermediate. Each electron thus transfers from the FMNH2 to an Fe-S cluster, from the Fe-S cluster to ubiquinone (Q). Transfer of the first electron results in the free-radical (semiquinone) form of Q, and transfer of the second electron reduces the semiquinone form to the ubiquinol form, QH2. During this process, four protons are translocated from the mitochondrial matrix to the intermembrane space. [4] As the electrons become continuously oxidized and reduced throughout the complex an electron current is produced along the 180 Angstrom width of the complex within the membrane. This current powers the active transport of four protons to the intermembrane space per two electrons from NADH.[5]
Complex II[edit]
In Complex II (succinate dehydrogenase or succinate-CoQ reductase; EC 1.3.5.1) additional electrons are delivered into the quinone pool (Q) originating from succinate and transferred (via flavin adenine dinucleotide (FAD)) to Q. Complex II consists of four protein subunits: succinate dehydrogenase, (SDHA); succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, (SDHB); succinate dehydrogenase complex subunit C, (SDHC) and succinate dehydrogenase complex, subunit D, (SDHD). Other electron donors (e.g., fatty acids and glycerol 3-phosphate) also direct electrons into Q (via FAD). Complex 2 is a parallel electron transport pathway to complex 1, but unlike complex 1, no protons are transported to the intermembrane space in this pathway. Therefore, the pathway through complex 2 contributes less energy to the overall electron transport chain process.
Complex III[edit]
In Complex III (cytochrome bc1 complex or CoQH2-cytochrome c reductase; EC 1.10.2.2), the Q-cycle contributes to the proton gradient by an asymmetric absorption/release of protons. Two electrons are removed from QH2 at the QO site and sequentially transferred to two molecules of cytochrome c, a water-soluble electron carrier located within the intermembrane space. The two other electrons sequentially pass across the protein to the Qi site where the quinone part of ubiquinone is reduced to quinol. A proton gradient is formed by one quinol (2H+2e-) oxidations at the Qo site to form one quinone (2H+2e-) at the Qi site. (in total four protons are translocated: two protons reduce quinone to quinol and two protons are released from two ubiquinol molecules).
 QH2 + 2 cytochrome c (FeIII) + 2 H+in → Q + 2 cytochrome c (FeII) + 4 H+out

When electron transfer is reduced (by a high membrane potential or respiratory inhibitors such as antimycin A), Complex III may leak electrons to molecular oxygen, resulting in superoxide formation.
Complex IV[edit]
In Complex IV (cytochrome c oxidase; EC 1.9.3.1), sometimes called cytochrome AA3, four electrons are removed from four molecules of cytochrome c and transferred to molecular oxygen (O2), producing two molecules of water. At the same time, eight protons are removed from the mitochondrial matrix (although only four are translocated across the membrane), contributing to the proton gradient. The activity of cytochrome c oxidase is inhibited by cyanide.
Coupling with oxidative phosphorylation[edit]
Depiction of ATP synthase, the site of oxidative phosphorylation to generate ATP.
According to the chemiosmotic coupling hypothesis, proposed by Nobel Prize in Chemistry winner Peter D. Mitchell, the electron transport chain and oxidative phosphorylation are coupled by a proton gradient across the inner mitochondrial membrane. The efflux of protons from the mitochondrial matrix creates an electrochemical gradient (proton gradient). This gradient is used by the FOF1 ATP synthase complex to make ATP via oxidative phosphorylation. ATP synthase is sometimes described as Complex V of the electron transport chain.[6] The FO component of ATP synthase acts as an ion channel that provides for a proton flux back into the mitochondrial matrix. It is composed of a, b and c subunits. Protons in the inter-membranous space of mitochondria first enters the ATP synthase complex through a subunit channel. Then protons move to the c subunits.[7] The number of c subunits it has determines how many protons it will require to make the FO turn one full revolution. For example, in humans, there are 8 c subunits, thus 8 protons are required.[8] After c subunits, protons finally enters matrix using a subunit channel that opens into the mitochondrial matrix.[7] This reflux releases free energy produced during the generation of the oxidized forms of the electron carriers (NAD+ and Q). The free energy is used to drive ATP synthesis, catalyzed by the F1 component of the complex.[9]
Coupling with oxidative phosphorylation is a key step for ATP production. However, in specific cases, uncoupling the two processes may be biologically useful. The uncoupling protein, thermogenin—present in the inner mitochondrial membrane of brown adipose tissue—provides for an alternative flow of protons back to the inner mitochondrial matrix. This alternative flow results in thermogenesis rather than ATP production.[10] Synthetic uncouplers (e.g., 2,4-dinitrophenol) also exist, and, at high doses, are lethal.[citation needed]
Summary[edit]
In the mitochondrial electron transport chain electrons move from an electron donor (NADH or QH2) to a terminal electron acceptor (O2) via a series of redox reactions. These reactions are coupled to the creation of a proton gradient across the mitochondrial inner membrane. There are three proton pumps: I, III, and IV. The resulting transmembrane proton gradient is used to make ATP via ATP synthase.
The reactions catalyzed by Complex I and Complex III work roughly at equilibrium. This means that these reactions are readily reversible, by increasing the concentration of the products relative to the concentration of the reactants (for example, by increasing the proton gradient). ATP synthase is also readily reversible. Thus ATP can be used to build a proton gradient, which in turn can be used to make NADH. This process of reverse electron transport is important in many prokaryotic electron transport chains.[11]
In bacteria[edit]
In eukaryotes, NADH is the most important electron donor. The associated electron transport chain is
NADH → Complex I → Q → Complex III → cytochrome c → Complex IV → O2 where Complexes I, III and IV are proton pumps, while Q and cytochrome c are mobile electron carriers. The electron acceptor is molecular oxygen.
In prokaryotes (bacteria and archaea) the situation is more complicated, because there are several different electron donors and several different electron acceptors. The generalized electron transport chain in bacteria is:
                     Donor Donor Donor ↓ ↓ ↓ dehydrogenase → quinone → bc1 → cytochrome ↓ ↓ oxidase(reductase) oxidase(reductase) ↓ ↓ Acceptor Acceptor

Note that electrons can enter the chain at three levels: at the level of a dehydrogenase, at the level of the quinone pool, or at the level of a mobile cytochrome electron carrier. These levels correspond to successively more positive redox potentials, or to successively decreased potential differences relative to the terminal electron acceptor. In other words, they correspond to successively smaller Gibbs free energy changes for the overall redox reaction Donor → Acceptor.
Individual bacteria use multiple electron transport chains, often simultaneously. Bacteria can use a number of different electron donors, a number of different dehydrogenases, a number of different oxidases and reductases, and a number of different electron acceptors. For example, E. coli (when growing aerobically using glucose as an energy source) uses two different NADH dehydrogenases and two different quinol oxidases, for a total of four different electron transport chains operating simultaneously.
A common feature of all electron transport chains is the presence of a proton pump to create a transmembrane proton gradient. Bacterial electron transport chains may contain as many as three proton pumps, like mitochondria, or they may contain only one or two. They always contain at least one proton pump.
Electron donors[edit]
In the present day biosphere, the most common electron donors are organic molecules. Organisms that use organic molecules as an energy source are called organotrophs. Organotrophs (animals, fungi, protists) and phototrophs (plants and algae) constitute the vast majority of all familiar life forms.
Some prokaryotes can use inorganic matter as an energy source. Such an organism is called a lithotroph ("rock-eater"). Inorganic electron donors include hydrogen, carbon monoxide, ammonia, nitrite, sulfur, sulfide, manganese oxide, and ferrous iron. Lithotrophs have been found growing in rock formations thousands of meters below the surface of Earth. Because of their volume of distribution, lithotrophs may actually outnumber organotrophs and phototrophs in our biosphere.
The use of inorganic electron donors as an energy source is of particular interest in the study of evolution. This type of metabolism must logically have preceded the use of organic molecules as an energy source.
Dehydrogenases[edit]
Bacteria can use a number of different electron donors. When organic matter is the energy source, the donor may be NADH or succinate, in which case electrons enter the electron transport chain via NADH dehydrogenase (similar to Complex I in mitochondria) or succinate dehydrogenase (similar to Complex II). Other dehydrogenases may be used to process different energy sources: formate dehydrogenase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, H2 dehydrogenase (hydrogenase), etc. Some dehydrogenases are also proton pumps; others funnel electrons into the quinone pool. Most dehydrogenases show induced expression in the bacterial cell in response to metabolic needs triggered by the environment in which the cells grow.[citation needed]
Quinone carriers[edit]
Quinones are mobile, lipid-soluble carriers that shuttle electrons (and protons) between large, relatively immobile macromolecular complexes embedded in the membrane. Bacteria use ubiquinone (the same quinone that mitochondria use) and related quinones such as menaquinone. Another name for ubiquinone is Coenzyme Q10.
Proton pumps[edit]
A proton pump is any process that creates a proton gradient across a membrane. Protons can be physically moved across a membrane; this is seen in mitochondrial Complexes I and IV. The same effect can be produced by moving electrons in the opposite direction. The result is the disappearance of a proton from the cytoplasm and the appearance of a proton in the periplasm. Mitochondrial Complex III uses this second type of proton pump, which is mediated by a quinone (the Q cycle).
Some dehydrogenases are proton pumps; others are not. Most oxidases and reductases are proton pumps, but some are not. Cytochrome bc1 is a proton pump found in many, but not all, bacteria (it is not found in E. coli). As the name implies, bacterial bc1 is similar to mitochondrial bc1 (Complex III).
Proton pumps are the heart of the electron transport process. They produce the transmembrane electrochemical gradient that enables ATP Synthase to synthesize ATP.
Cytochrome electron carriers[edit]
Cytochromes are pigments that contain iron. They are found in two very different environments.
Some cytochromes are water-soluble carriers that shuttle electrons to and from large, immobile macromolecular structures imbedded in the membrane. The mobile cytochrome electron carrier in mitochondria is cytochrome c. Bacteria use a number of different mobile cytochrome electron carriers.
Other cytochromes are found within macromolecules such as Complex III and Complex IV. They also function as electron carriers, but in a very different, intramolecular, solid-state environment.
Electrons may enter an electron transport chain at the level of a mobile cytochrome or quinone carrier. For example, electrons from inorganic electron donors (nitrite, ferrous iron, etc.) enter the electron transport chain at the cytochrome level. When electrons enter at a redox level greater than NADH, the electron transport chain must operate in reverse to produce this necessary, higher-energy molecule.
Terminal oxidases and reductases[edit]
When bacteria grow in aerobic environments, the terminal electron acceptor (O2) is reduced to water by an enzyme called an oxidase. When bacteria grow in anaerobic environments, the terminal electron acceptor is reduced by an enzyme called a reductase.
In mitochondria the terminal membrane complex (Complex IV) is cytochrome oxidase. Aerobic bacteria use a number of different terminal oxidases. For example, E. coli does not have a cytochrome oxidase or a bc1 complex. Under aerobic conditions, it uses two different terminal quinol oxidases (both proton pumps) to reduce oxygen to water.
Anaerobic bacteria, which do not use oxygen as a terminal electron acceptor, have terminal reductases individualized to their terminal acceptor. For example, E. coli can use fumarate reductase, nitrate reductase, nitrite reductase, DMSO reductase, or trimethylamine-N-oxide reductase, depending on the availability of these acceptors in the environment.
Most terminal oxidases and reductases are inducible. They are synthesized by the organism as needed, in response to specific environmental conditions.
Electron acceptors[edit]
Just as there are a number of different electron donors (organic matter in organotrophs, inorganic matter in lithotrophs), there are a number of different electron acceptors, both organic and inorganic. If oxygen is available, it is invariably used as the terminal electron acceptor, because it generates the greatest Gibbs free energy change and produces the most energy.[citation needed]
In anaerobic environments, different electron acceptors are used, including nitrate, nitrite, ferric iron, sulfate, carbon dioxide, and small organic molecules such as fumarate.
Since electron transport chains are redox processes, they can be described as the sum of two redox pairs. For example, the mitochondrial electron transport chain can be described as the sum of the NAD+/NADH redox pair and the O2/H2O redox pair. NADH is the electron donor and O2 is the electron acceptor.
Not every donor-acceptor combination is thermodynamically possible. The redox potential of the acceptor must be more positive than the redox potential of the donor. Furthermore, actual environmental conditions may be far different from standard conditions (1 molar concentrations, 1 atm partial pressures, pH = 7), which apply to standard redox potentials. For example, hydrogen-evolving bacteria grow at an ambient partial pressure of hydrogen gas of 10−4 atm. The associated redox reaction, which is thermodynamically favorable in nature, is thermodynamic impossible under "standard" conditions.[citation needed]
Summary[edit]
Bacterial electron transport pathways are, in general, inducible. Depending on their environment, bacteria can synthesize different transmembrane complexes and produce different electron transport chains in their cell membranes. Bacteria select their electron transport chains from a DNA library containing multiple possible dehydrogenases, terminal oxidases and terminal reductases. The situation is often summarized by saying that electron transport chains in bacteria are branched, modular, and inducible.
Photosynthetic[edit]
In oxidative phosphorylation, electrons are transferred from a low-energy electron donor (e.g., NADH) to an acceptor (e.g., O2) through an electron transport chain. In photophosphorylation, the energy of sunlight is used to create a high-energy electron donor and an electron acceptor. Electrons are then transferred from the donor to the acceptor through another electron transport chain.
Photosynthetic electron transport chains have many similarities to the oxidative chains discussed above. They use mobile, lipid-soluble carriers (quinones) and mobile, water-soluble carriers (cytochromes, etc.). They also contain a proton pump. It is remarkable that the proton pump in all photosynthetic chains resembles mitochondrial Complex III.
Photosynthetic electron transport chains are discussed in greater detail in the articles Photophosphorylation, Photosynthesis, Photosynthetic reaction center and Light-dependent reaction.
Summary[edit]
Electron transport chains are redox reactions that transfer electrons from an electron donor to an electron acceptor. The transfer of electrons is coupled to the translocation of protons across a membrane, producing a proton gradient. The proton gradient is used to produce useful work. About 30 work units are produced per electron transport.
See also[edit]
CoRR hypothesis
Electron equivalent
Hydrogen hypothesis
Respirasome
References[edit]
Jump up ^ Murray, Robert K.; Daryl K. Granner; Peter A. Mayes; Victor W. Rodwell (2003). Harper's Illustrated Biochemistry. New York, NY: Lange Medical Books/ MgGraw Hill. p. 96. ISBN 0-07-121766-5.
Jump up ^ Karp, Gerald (2008). Cell and Molecular Biology (5th ed.). Hoboken, NJ: John Wiley & Sons. p. 194. ISBN 978-0-470-04217-5.
Jump up ^ Lauren, Biochemistry, Johnson/Cole, 2010, pp 598-611
Jump up ^ Garrett & Grisham, Biochemistry, Brooks/Cole, 2010, pp 598-611
Jump up ^ Garret and Grisham (2016). biochemistry. University of Virginia. p. 687. ISBN 978-1-305-57720-6.
Jump up ^ Jonckheere, An I.; Smeitink, Jan A. M.; Rodenburg, Richard J. T. (2017-03-10). "Mitochondrial ATP synthase: architecture, function and pathology". Journal of Inherited Metabolic Disease. 35 (2): 211–225. doi:10.1007/s10545-011-9382-9. ISSN 0141-8955. PMC 3278611  . PMID 21874297.
^ Jump up to: a b Garrett, Reginald H.; Grisham, Charles M. (2012). Biochemistry (5th ed.). Cengage learning. p. 664. ISBN 1-133-10629-3.
Jump up ^ Fillingame, Robert H; Angevine, Christine M; Dmitriev, Oleg Y (2003-11-27). "Mechanics of coupling proton movements to c-ring rotation in ATP synthase". FEBS Letters. 555 (1): 29–34. doi:10.1016/S0014-5793(03)01101-3. ISSN 1873-3468.
Jump up ^ Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2002-01-01). "A Proton Gradient Powers the Synthesis of ATP".
Jump up ^ Cannon, Barbara; Nedergaard, Jan (2004-01-01). "Brown Adipose Tissue: Function and Physiological Significance". Physiological Reviews. 84 (1): 277–359. doi:10.1152/physrev.00015.2003. ISSN 0031-9333. PMID 14715917.
Jump up ^ Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter (2002-01-01). "Electron-Transport Chains and Their Proton Pumps".
Fenchel T; King GM; Blackburn TH (September 2006). Bacterial Biogeochemistry: The Ecophysiology of Mineral Cycling (2nd ed.). Elsevier. ISBN 978-0-12-103455-9.
Lengeler JW (January 1999). Drews G; Schlegel HG, eds. Biology of the Prokaryotes. Blackwell Science. ISBN 978-0-632-05357-5.
Nelson DL; Cox MM (April 2005). Lehninger Principles of Biochemistry (4th ed.). W. H. Freeman. ISBN 978-0-7167-4339-2.
Nicholls DG; Ferguson SJ (July 2002). Bioenergetics 3. Academic Press. ISBN 978-0-12-518121-1.
Stumm W; Morgan JJ (1996). Aquatic Chemistry (3rd ed.). John Wiley & Sons. ISBN 978-0-471-51185-4.
Thauer RK; Jungermann K; Decker K (March 1977). "Energy conservation in chemotrophic anaerobic bacteria". Bacteriol Rev. 41 (1): 100–80. PMC 413997  . PMID 860983.
White D. (September 1999). The Physiology and Biochemistry of Prokaryotes (2nd ed.). Oxford University Press. ISBN 978-0-19-512579-5.
Voet D; Voet JG (March 2004). Biochemistry (3rd ed.). John Wiley & Sons. ISBN 978-0-471-58651-7.
Kim HS.; Patel, K; Muldoon-Jacobs, K; Bisht, KS; Aykin-Burns, N; Pennington, JD; Van Der Meer, R; Nguyen, P; et al. (January 2010). "SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress". Cancer Cell. 17 (1): 41–52. doi:10.1016/j.ccr.2009.11.023. PMC 3711519  . PMID 20129246.
External links[edit]
Electron Transport Chain Complex Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
Khan Academy, video lecture
UMich Orientation of Proteins in Membranes families/superfamily-3 - Complexes with cytochrome b-like domains
UMich Orientation of Proteins in Membranes families/superfamily-4 - Bacterial and mitochondrial cytochrome c oxidases
UMich Orientation of Proteins in Membranes families/superfamily-2 - Photosynthetic reaction centers and photosystems
UMich Orientation of Proteins in Membranes families/superfamily-78 - Cytochrome PORN renodoxin reductase
UMich Orientation of Proteins in Membranes families/superfamily-130 - Electron transfer flavoproteins
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values: سلسلة نقل الإلكترون – Arabic

values: Електрон-транспортна верига – Bulgarian

values: Cadena de transport d'electrons – Catalan

values: Cadena de transporte de electrones – Spanish

values: زنجیره انتقال الکترون – Persian

values: Chaîne de transport d'électrons – French

values: Cadea de transporte electrónico – Galician

values: 전자전달계 – Korean

values: Catena di trasporto degli elettroni – Italian

values: Дыхательная цепь переноса электронов – Russian

values: Electron transport chain – Simple English

values: Lanac transporta elektrona – Serbo-Croatian

values: ลูกโซ่ของการขนส่งอิเล็กตรอน – Thai

values: Електронтранспортний ланцюг – Ukrainian

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