text:
Let My Love Open the Door
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"Let My Love Open the Door"
Single by Pete Townshend
from the album Empty Glass
B-side
"Greyhound Girl"
Released
June 4, 1980 (US)
Format
7"
Recorded
March 1980
Genre
Art rock, new wave
Length
2:44
Label
Atco Records
Songwriter(s)
Pete Townshend
Producer(s)
Pete Townshend, Chris Thomas
Pete Townshend UK singles chronology
"Rough Boys"
(1980) "Let My Love Open the Door"
(1980) "Keep on Working"
(1980)
"Rough Boys"
(1980) "Let My Love Open the Door"
(1980) "Keep on Working"
(1980)
Pete Townshend US singles chronology
"Keep Me Turning"
(1977)
[with Ronnie Lane] Keep Me Turning1977 "Let My Love Open the Door"
(1980) Let My Love Open the Door1980 "A Little Is Enough"
(1980) A Little Is Enough1980
"Let My Love Open the Door" is a song written and performed by Pete Townshend from his 1980 album Empty Glass. It reached the top ten in the United States in that same year, reaching number nine.[1][2] It reached number five in Canada.[3]
Contents
[hide]
1 Background
2 Chart performance
2.1 Weekly charts
2.2 Year-end charts
3 Personnel
4 Covers
5 List of Films, TV Shows, and Other Media featuring the track
6 References
7 External links
Background[edit]
Although Townshend is a devotee to the religious guru Meher Baba, he claimed in the liner notes of his Anthology CD that "Jesus sings" on the track.[4]
"Let My Love Open the Door" was released as the second single from Empty Glass in Britain, where it was backed with the non-album tracks "Classified" and "Greyhound Girl." The song was a minor British hit, reaching #46.[5] The song saw more success when it was released as the debut single from Empty Glass in America, where the song reached #9.[6] It was Pete Townshend's only solo top 10 hit on the Billboard Hot 100, but The Who's song "I Can See For Miles," which was written by Townshend, reached the same position on the chart 13 years earlier.
Initially, Townshend's manager despised the track due to it "not sounding like Townshend," and wanted it to be removed from Empty Glass.[4] However, upon the song's chart success, his manager called to apologize.
Despite the song's critical and commercial success, Pete Townshend did not consider it one of his best songs. He told Rolling Stone in an interview that "Let My Love Open the Door" was "just a ditty," also claiming that he preferred his minor US hit "A Little Is Enough" from the same album.[4]
In 1996, Townshend released a new version of the song, called "the E. Cola mix", turning the song into a ballad. This version appeared in different television shows and film soundtracks.
Chart performance[edit]
Weekly charts[edit]
Chart (1980)
Peak
position
Canada RPM 100[3] 5
UK Singles Chart 46
U.S. Billboard Hot 100 [7] 9
U.S. Cash Box Top 100 11
Year-end charts[edit]
Chart (1980)
Rank
Canada [8] 35
U.S. Billboard Hot 100 [9] 59
U.S. Cashbox 92
Personnel[edit]
Pete Townshend: vocals, guitars, synths
John "Rabbit" Bundrick: "straight" keyboards
Simon Phillips: drums
Tony Butler: bass guitar
Ted Jensen - mastering engineer
Covers[edit]
A version of this song by Luminate appears on The Covers EP.[10]
It was also covered by M. Ward (for the 2005 Starbucks compilation album, Sweetheart 2005: Love Songs)
Christian rock group Audio Adrenaline covered this song on their 1999 album Underdog.
Natalie Imbruglia covered the song on her album Male released in 2015.
Great Big Sea covered the song on their 2012 album XX.
Roger Daltrey covered the song in 2015 for a campaign involving Teen Cancer America and First Citizens Bank.[11] A full version was released in February 2016, with all proceeds going to Teen Cancer America.
The group Rogue Wave also covered it in "Cover me" released in 2017.
List of Films, TV Shows, and Other Media featuring the track[edit]
The song has been used frequently in film, most notably the comedy genre, often as trailer music for movies such as Jerry Maguire and How Do You Know, and then as end credit song for Mr. Deeds in 2002; Jersey Girl and Along Came Polly, both in 2004. It was featured in the following films and TV series:
Look Who's Talking (1989)
Grosse Pointe Blank as "E. Cola Mix" (1997)
Mr. Deeds (2002)
Jersey Girl as "E. Cola Mix" (2004)
Along Came Polly (2004)
Click (in trailers) (2006)
Dan in Real Life (2007)
Doctors (soap opera), season 11, episode 106 (2009)
Old Dogs (2009)
How Do You Know (in trailers) (2010)
Take Me Home Tonight as "E. Cola Mix" (2011)
Red Dog (2011)
Hit and Run (2012)
The Newsroom (2012) - cover by Luminate used in the second season finale, "Election Night, Part II" (September 15, 2013)
Californication, season 7, episode 1 (April 13, 2014)
The Goldbergs, season 1 "Why're You Hitting Yourself?" (2013) the "E. Cola Mix" played at end before credits. Also played in Season 4, Episode 15 "So Swayze It's Crazy" (2017).
A cover of the song by Stacey Markus is used at the end of episode nine ("The Invitation") of the 2015 Netflix original series Grace and Frankie, starring Jane Fonda and Lily Tomlin.
The song is featured in a Walmart Christmas holiday television commercial which started airing in early December 2017.[12]
Lethal Weapon (TV series), season 2, episode 9 "Fools Rush In" play the song performed by "Rogue wave" (2017). [13]
References[edit]
Jump up ^ Unterberger, Richie (2012-06-14). "Let My Love Open the Door". Rolling Stone. Retrieved 2016-10-16.
Jump up ^ "Pete Townshend, 'Empty Glass' | 100 Best Albums of the Eighties". Rolling Stone. 1989-11-16. Retrieved 2016-10-16.
^ Jump up to: a b Bac-lac.gc.ca
^ Jump up to: a b c "Let My Love Open the Door". Songfacts.com.
Jump up ^ "Pete Townshend UK charts". Official Charts.
Jump up ^ "Pete Townshend US charts". Billboard.
Jump up ^ Joel Whitburn's Top Pop Singles 1955-1990 - ISBN 0-89820-089-X
Jump up ^ Collectionscanada.gc.ca Archived 2016-04-25 at the Wayback Machine.
Jump up ^ Musicoutfitters.com
Jump up ^ "The Covers EP: Various artists: MP3 Downloads". Amazon.com. Retrieved 2016-10-16.
Jump up ^ "Help us open the door to better cancer care | #LetMyLoveOpenTheDoor". Firstcitizens.com. Retrieved 2016-10-16.
Jump up ^ "Walmart TV Commercial, 'Christmas Like a Rock Star' Song by Pete Townshend". Ispot.tv. Retrieved December 6, 2017.
Jump up ^ "Leathal Weapon (TV series) "Fools Rush" Soundtracks (2017)". Imdb.com. 2017-05-12. Retrieved 2018-03-30.
External links[edit]
Lyrics of this song at MetroLyrics
[hide]
v
t
e
Pete Townshend
Discography
Studio albums
Who Came First
Rough Mix (w/ Ronnie Lane)
Empty Glass
All the Best Cowboys Have Chinese Eyes
White City: A Novel
The Iron Man: A Musical
Psychoderelict
Classic Quadrophenia
Meher Baba tribute albums
(w/ Ronnie Lane et al.)
Happy Birthday
I Am
With Love
O' Parvardigar
Live albums
Deep End Live! (w/ Deep End)
A Benefit for Maryville Academy
Live: The Empire
Live: Sadler's Wells
Live: The Fillmore
The Oceanic Concerts (w/ Raphael Rudd)
Live: La Jolla Playhouse 2001
Pete Townshend Live BAM 1993
Live: Brixton Academy '85
Compilations
Scoop
Another Scoop
The Best of Pete Townshend
Scoop 3
Scooped
Lifehouse Chronicles
Lifehouse Elements
Anthology
Truancy: The Very Best of Pete Townshend
Singles
"Let My Love Open the Door"
"Rough Boys"
"A Little Is Enough"
"Keep on Working"
"Face Dances, Pt. 2"
"Face the Face"
"Give Blood"
"English Boy"
Other Songs
"Parvardigar"
"Somebody Saved Me"
"Slit Skirts"
"White City Fighting"
"Fire"
DVDs
Lifehouse (video)
Live In New York Feat. Psychoderelict
O Parvardigar
Related articles
Songs
Songs Written
Albums
Peter Meaden
The Who
Deep End
Tommy (film)
The Who's Tommy
Tommy (EP)
Tommy (soundtrack)
The Boy Who Heard Music
Quadrophenia (musical)
Quadrophenia (film)
Quadrophenia (soundtrack)
The Lifehouse Method
Horse's Neck
Who I Am
Eel Pie Publishing
Eel Pie Studios
Double O
Cliff Townshend
Emma Townshend
Simon Townshend
The Wick
Ashdown House, Oxfordshire
The Boathouse, Twickenham
Chapel House, Twickenham
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Renaming of cities in India
From Wikipedia, the free encyclopedia
Jump to: navigation, search
The renaming of cities in India started in 1947 following the end of the British imperial period. Several changes were politically controversial, and not all proposed changes were implemented. Each had to be approved by the central government in New Delhi.
The renaming of states and territories in India has also taken place, but until recently with actual substantial name changes in both local language and in English such as the old British state name of Travancore-Cochin to Kerala (1956). The most notable recent exceptions are Indian English spelling-changes of Orissa to Odisha (March 2011)[1] and the Union Territory of Pondicherry (which includes the City of Pondicherry) to Puducherry.
Contents
[hide]
1 Renaming in local languages
2 Renaming in English
2.1 Change in official English spelling
2.2 Realignment of the official Indian English name to an alternative local name
2.3 Adoption of name changes in India and overseas
3 Important examples
3.1 States
3.2 Cities
4 Proposed changes
4.1 States and Union territories
4.2 Towns
5 Need for unification of spelling
6 See also
7 References
8 External links
Renaming in local languages[edit]
In the post-colonial era, several Indian states' names were changed. Some of these changes coincided with the States Reorganisation Act of 1956, a major reform of the boundaries of India's states and territories that organised them along linguistic lines. At this time, for example, Travancore-Cochin was renamed Kerala. Later state name changes include the reorganisation of Madhya Bharat into Madhya Pradesh in 1959;[2] and the renamings of the Madras State to Tamil Nadu in 1969, of the Mysore State to Karnataka in 1973, and of Uttaranchal to Uttarakhand in 2007.
Name changes have varied with respect to the levels of language at which they have been applied, and also accepted. Some of these local name changes were changes made in all languages: the immediate local name, and also all India's other languages. An example of this is the renaming of predominantly Hindi-speaking Uttaranchal (Hindi: उत्तराञ्चल) to a new local Hindi name (Hindi: उत्तराखण्ड Uttarakhand). Other changes were only changes in some of the indigenous languages. For example, the renaming of the Madras Presidency to Madras State in 1947 and then Tamil Nadu in 1969 required non-Tamil speakers to change from an approximation of the British name (Tamil: மதராஸ் மாகாணம் Madras Presidency, then Madras State Tamil: மதராஸ் மாநிலம்) to a native Tamil name (Tamil: தமிழ்நாடு Tamil Nadu, "Tamil land").
In general, changes to the local names of cities in the indigenous languages are less common. However, a change in English may sometimes also be a reflection of changes in other Indian languages other than the specific local one. For example, the change of Madras (Tamil: மதராஸ் Madras) to Chennai (Tamil: சென்னை Chennai) was reflected in many of India's languages, and incidentally in English, while the Tamil endonym had always been Chennai and remained unaffected by the change.
Renaming in English[edit]
Change in official English spelling[edit]
The renaming of cities is often specifically from English to Indian English in connection with that dialect's internal reforms. In other words, the city itself is not actually renamed in the local language, and the local name (or endonym) in the indigenous languages of India does not change, but the official spelling in Indian English is amended. An example is the change from English "Calcutta" to English "Kolkata" – the local Bengali name (কলকাতা Kôlkata) did not change. Such changes in English spelling may be in order to better reflect a more accurate phonetic transliteration of the local name, or may be for other reasons. In the early years after Indian independence, many name changes were effected in northern India for English spellings of Hindi place names that had simply been romanised inconsistently by the British administration – such as the British spelling "Jubbulpore," renamed "Jabalpur" (जबलपुर) among the first changes in 1947. These changes did not generate significant controversy. More recent and high-profile changes – including renaming such major cities as Calcutta to Kolkata – have generated greater controversy.[3] Since independence, such changes have typically been enacted officially by legislation at local or national Indian government level, and may or may not then be adopted by the Indian media, particularly the influential Indian press. In the case of smaller towns and districts which were less notable outside and inside India, and where a well known English name (or exonym) could not be said to exist, older spellings used under British India may not have had any specific legislation other than changes in practice on the romanisation of indigenous Indian language names.
Realignment of the official Indian English name to an alternative local name[edit]
Aside from changes to the official English spellings of local names there have also been renaming proposals to realign the official name, hence the English name with an alternative local name. Ethnically sensitive examples include the proposals by the Bharatiya Janata Party (1990, 2001) to rename Ahmedabad to Karnavati[4] and Allahabad to Prayag. These two proposals are changes from the Muslim (or Mughal) name to a Hindu native name. These can be represented as a change from Urdu language to Hindi language, but since the two languages are variants of Hindustani the proposal is effectively a cultural and ethno-religious proposal rather than a linguistic one.[5]
Adoption of name changes in India and overseas[edit]
Official name changes naturally take place quickly if not immediately in official government sources.[6] Adoption may be slower among the media in India and abroad, and among Indian authors.[7][8][9]
Important examples[edit]
Main article: List of renamed places in India
States[edit]
Travancore-Cochin → Kerala (1 November 1956).
Madhya Bharat → Madhya Pradesh (1 November 1959)
Madras State → Tamil Nadu (14 January 1969)
Mysore State → Karnataka (1 November 1973)
Uttaranchal → Uttarakhand (1 January 2007)
Orissa → Odisha (4 November 2011)
Cities[edit]
Notable city names that were officially changed by legislation after independence include:
Jabalpur (Hindi: जबलपुर), from Jubbulpore, respelled in 1947
Jajmau (Hindi: जाजमऊ), from Jajesmow, respelled in 1948 [10]
Kanpur (Hindi: कानपुर), from Cawnpore, respelled in 1948
Vadodara (Gujarati: વડોદરા), from Baroda, respelled in 1974
Thiruvananthapuram (Malayalam: തിരുവനന്തപുരം), from Trivandrum, respelled in 1991
Mumbai (Marathi: मुंबई), from Bombay, renamed in 1995 [11]
Kochi (Malayalam: കൊച്ചി), from Cochin, respelled in 1996
Chennai (Tamil: சென்னை), from Madras, renamed in 1996
Kolkata (Bengali: কলকাতা), from Calcutta, respelled in 2001
Kadapa (Telugu: కడప), from Cuddapah, respelled in 2005
Puducherry (Tamil: புதுச்சேரி), from Pondicherry, renamed in 2006
Bengaluru (Kannada: ಬೆಂಗಳೂರು), from Bangalore, respelled in 2007 [12]
Belagavi from Belgaum in 2014 [13][14]
Tumakuru from Tumkur in 2014
Hubballi from Hubli in 2014
Shivamogga from Shimoga in 2014
Hosapete from Hospet in 2014
Mysuru from Mysore in 2014
Kalaburagi from Gulbarga in 2014
Chikkamagaluru from Chikmagalur
Vijapura from Bijapur in 2014
Ballari from Bellary in 2014
Mangaluru from Mangalore in 2014
Rajahmahendravaram from Rajahmundry in 2015
Gurugram from Gurgaon in 2016
For others, by state order, see list of renamed Indian cities and states.
Alappuzha, from Alleppey
Guwahati (Assamese: গুৱাহাটী), from Gauhati
Indore, from Indhur
Kanchipuram from Kāñci-pura And Conjevaram
Kannur, from Cannanore
Kollam, from Quilon
Koyilandy, from Quilandi
Kozhikode, from Calicut
Kumbakonam from ancient name Kudanthai
Mayiladuthurai from Mayavaram ancient name Mayuram
Narmada, from Nerbudda
Nagaon (Assamese: নগাওঁ), from Nowgong
Palakkad, from Palghat
Panaji, from Panjim
Pune, from Poona
Ramanathapuram, from Ramnad
Sagar, from Saugor
Shimla, from Simla
Thalassery, from Tellicherry
Thanjavur, from ancient name Tanjore
Thoothukudi, from Tuticorin
Thrissur, from Trichur
Tindivanam, from Tinthirivanam
Tiruchirapalli, from Trichinopoly and its short form Trichy
Tirunelveli, from Tinnevelly
Tiruvallikeni, from Triplicane
Udhagamandalam, from Ootacamund and its short form Ooty
Viluppuram, from Vizhupparaiyar And Vizhimaa Nagaram
Varanasi, from Benares
Vatakara, from Badagara
Virudhachalam, from Vriddhachalam ancient name Thirumudhukundram
Vijayawada, from Bejawada
Visakhapatnam, from Waltair, and before that Vizagapatnam and its short form Vizag
Town names that derive from ancient names:
Mandi, derived from Mandav Nagar [15]
Nellore, in ancient times Simhapuri [16]
Proposed changes[edit]
Several other changes have been proposed for states and towns.
States and Union territories[edit]
Goa to Govapuri [17]
Kerala to Keralam
Nagaland to Naganchi [18]
West Bengal to Bengal
Towns[edit]
Ahmedabad to Karnavati
Allahabad to Prayagraj[19]
Aurangabad to Sambhajinagar
Bhopal to Bhojpal [20]
Hyderabad to Bhagyanagar
Mahabubabad to Manukota
Mahbubnagar to Palamuru
Need for unification of spelling[edit]
India has various local languages. Even (Romanised) English spellings in long and wide use often vary depending upon which government department or agency uses them. To the point, a few examples are Quilandy vs. Koyilandy, Canannore vs. Kannur, and Rangiya vs. Rangia. Different departments of the government may have used official spellings in use at the time, while locations associated with Indian railways mostly maintained British-era spellings. The confusion inherent in such variations has often resulted in serious consequences like people having two "different" addresses (theoretically designating the same place) in their official records leading to legal disputes, or one house having residents of different house addresses due to differing place names. Many people argue that such confusion can lead to indeterminate and/or unintended consequences [21]
See also[edit]
India portal
List of renamed Indian cities and states
Renaming in South Africa
References[edit]
Jump up ^ India and the World Bank: The Politics of Aid and Influence - Page 126 Jason A. Kirk - 2011 "Orissa (Note: This state was officially renamed Odisha in March 2011)"
Jump up ^ The Hindu Nationalist Movement and Indian Politics, 1925 to the 1990s. - Page 134 Christophe Jaffrelot 1999 - "The new state included Madhya Bharat, the Bhopal region, the former Vindhya Pradesh, Mahakoshal and Chhattisgarh (the last two regions forming the Hindi-speaking parts in the former Madhya Pradesh; see map, pp. xxii-xxiii)."
Jump up ^ Mira Kamdar Planet India: How the Fastest Growing Democracy Is Transforming ... 2007 Author's introduction Page xi "India's information-technology capital's new name, should it be adopted, will mean “town of boiled beans.” The name changes are not without controversy among Indians. In several instances, the name change represents a struggle between a cosmopolitan elite and a local, regional-language populace over defining the city in ways that go far beyond a simple change of name."
Jump up ^ Steven I. Wilkinson Votes and Violence: Electoral Competition and Ethnic Riots in India 2006 Page 23 "The BJP proposed in 1990 and 2001 that Ahmedabad be renamed "Karnavati." Hindu, June 1 1, 2001. Similar proposals have been made to rename Allahabad "Prayag."
Jump up ^ Cosmopolitanism - Page 73 Carol A. Breckenridge, Sheldon Pollock, Homi K. Bhabha - 2002 "In one sense, the decision to officialise the name Mumbai is part of a widespread Indian pattern of replacing names associated with colonial rule with names associated with local, national, and regional heroes. It is an indigenizing toponymic "
Jump up ^ Reserve Bank of India's instructions for banks & banking operations Reserve Bank of India 2001 Page 713 "The new name "Mumbai" should be reflected in both English and Hindi and the change in name is to be brought about in all official communications, name plates, sign boards, office seals, rubber stamps, etc."
Jump up ^ Perveez Mody The Intimate State: Love-Marriage and the Law in Delhi Page 59 - 2008 "Throughout this book, I refer to India's commercial capital as Bombay rather than Mumbai. ... I am well aware of the name-change effected by an Act of the Indian Parliament in 1997 that made the city officially 'Mumbai'. ... It is the same convention I adopt when referring to Calcutta rather than Kolkata."
Jump up ^ Pingali Sailaja Indian English Page 16 2009 "Bombay is now called Mumbai, Madras is now Chennai and Calcutta is Kolkata, in an attempt to de-anglicise them. In this work, the earlier names are retained since these names were used during the period that we mostly cover."
Jump up ^ Calcutta: A Cultural and Literary History - Page 3 Krishna Dutta - 2003 "nationalist stance, like Bombay, which changed its name to Mumbai, or Madras, which has become the unrecognisable Chennai, Calcutta has preferred a comparatively minor name change, which frankly is a bit of a multicultural mishmash."
Jump up ^ "David Rumsey: Geographical Searching with MapRank Search (beta)". Rumsey.mapranksearch.com. Retrieved 2012-08-15.
Jump up ^ Beam, Christopher (2006-07-12). "How Bombay became Mumbai. - Slate Magazine". Slate.com. Retrieved 2012-08-15.
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Jump up ^ Gazetteer of the Nellore District: Brought Up to 1938 - Page 151 Government Of Madras Staff, Government of Madras - 1942 "... of the Ramayana (2000 — 1500 BC) was a dense jungle, while the town of Nellore, which came into existence only several centuries later, was known as Simhapuri (Lion's town), from the supposed existence of lions in the adjacent forests."
Jump up ^ "Goa to become Govapuri".
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Jump up ^ http://www.igovernment.in/opinion/41631/merging-npr-uid?source=igov
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Renaming roads: A 'meaningless' exercise
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ATP synthase
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ATP Synthase
Molecular model of ATP synthase determined by X-ray crystallography. Stator is not shown here.
Identifiers
EC number
3.6.3.14
CAS number
9000-83-3
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IntEnz view
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BRENDA entry
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KEGG entry
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metabolic pathway
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ATP synthase is an enzyme that creates the energy storage molecule adenosine triphosphate (ATP). ATP is the most commonly used "energy currency" of cells for most organisms. It is formed from adenosine diphosphate (ADP) and inorganic phosphate (Pi). The overall reaction catalyzed by ATP synthase is:
ADP + Pi + H+out ⇌ ATP + H2O + H+in
The formation of ATP from ADP and Pi is energetically unfavorable and would normally proceed in the reverse direction. In order to drive this reaction forward, ATPase couples ATP synthesis during cellular respiration to an electrochemical gradient created by the difference in proton (H+) concentration across the mitochondrial membrane in eukaryotes or the plasma membrane in bacteria. During photosynthesis in plants, ATP is synthesized by ATPase using a proton gradient created in the thylakoid lumen through the thylakoid membrane and into the chloroplast stroma.
ATP synthase consists of two main subunits, FO and F1, which has a rotational motor mechanism allowing for ATP production.[1][2] Because of its rotating subunit ATP Synthase is a molecular machine.
Contents
[hide]
1 Nomenclature
2 Structure and function
2.1 F1 region
2.2 FO region
3 Binding model
4 Physiological role
5 Evolution
6 In different species
6.1 E. coli
6.2 Yeast
6.3 Plant
6.4 Bovine
6.5 Human
7 See also
8 References
9 Further reading
10 External links
Nomenclature[edit]
The F1 fraction derives its name from the term "Fraction 1" and FO (written as a subscript letter "o", not "zero") derives its name from being the binding fraction for oligomycin, a type of naturally-derived antibiotic that is able to inhibit the FO unit of ATP synthase.[3][4] These functional regions consist of different protein subunits — refer to tables.
Structure and function[edit]
Bovine mitochondrial ATP synthase. The FO, F1, axle, and stator regions are color coded magenta, green, orange, and cyan respectively.[5][6]
Simplified model of FOF1-ATPase alias ATP synthase of E. coli. Subunits of the enzyme are labeled accordingly.
Rotation engine of ATP synthase.
Located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two regions FO and F1. FO causes rotation of F1 and is made of c-ring and subunits a, b, d, F6. F1 is made of α , β , γ , δ {\displaystyle \alpha ,\beta ,\gamma ,\delta } subunits. F1 has a water soluble par that can hydrolyze ATP. FO on the other hand has mainly hydrophobic regions. FO F1 creates a pathway for protons movement across the membrane.[7]
F1 region[edit]
The F1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. Subunits α {\displaystyle \alpha } and β {\displaystyle \beta } make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP.
Other three subunits catalyze the ATP synthesis. The other F1 subunits γ , δ , ϵ {\displaystyle \gamma ,\delta ,\epsilon } are a part of a rotational motor mechanism. γ {\displaystyle \gamma } subunit allows β {\displaystyle \beta } to go though conformational changes, i.e closed, half open and open states allows for ATP to be bound and released once synthesized. The F1 particle is large and can be seen in the transmission electron microscope by negative staining.[8] These are particles of 9 nm diameter that pepper the inner mitochondrial membrane.
F1 - Subunits
Subunit
Human Gene
alpha ATP5A1, ATPAF2
beta ATP5B, ATPAF1, C16orf7
gamma ATP5C1
delta ATP5D
epsilon ATP5E
FO region[edit]
FO subunit F6 from the peripheral stalk region of ATP synthase.[9]
Fo is a water insoluble protein with eight subunits and transmembrane ring. The ring has a tetramer shape with protein helix loop helix that goes though conformational change when protonated and deprotonated allowing to push neighboring subunits to rotate causing the spinning of FO which then affects conformation of F1 also, resulting on switching of states of alpha and beta subunits. The FO region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane. It consists of three main subunits a, b, and c, and (in humans) six additional subunits, d, e, f, g, F6, and 8 (or A6L). An atomic model for the dimeric yeast FO region was determined by cryo-EM at an overall resolution of 3.6 Å [10]
FO-Main subunits
Subunit
Human Gene
a ATP6
b ATP5F1
c ATP5G1, ATP5G2, ATP5G3
Binding model[edit]
Mechanism of ATP synthase. ADP and Pi (pink) shown being combined into ATP (red), and the rotating γ (gamma) subunit in black causing conformation.
Depiction of ATP synthase using the chemiosmotic proton gradient to power ATP synthesis through oxidative phosphorylation.
In the 1960s through the 1970s, Paul Boyer, a UCLA Professor, developed the binding change, or flip-flop, mechanism theory, which postulated that ATP synthesis is dependent on a conformational change in ATP synthase generated by rotation of the gamma subunit. The research group of John E. Walker, then at the MRC Laboratory of Molecular Biology in Cambridge, crystallized the F1 catalytic-domain of ATP synthase. The structure, at the time the largest asymmetric protein structure known, indicated that Boyer's rotary-catalysis model was, in essence, correct. For elucidating this, Boyer and Walker shared half of the 1997 Nobel Prize in Chemistry.
The crystal structure of the F1 showed alternating alpha and beta subunits (3 of each), arranged like segments of an orange around a rotating asymmetrical gamma subunit. According to the current model of ATP synthesis (known as the alternating catalytic model), the transmembrane potential created by (H+) proton cations supplied by the electron transport chain, drives the (H+) proton cations from the intermembrane space through the membrane via the FO region of ATP synthase. A portion of the FO (the ring of c-subunits) rotates as the protons pass through the membrane. The c-ring is tightly attached to the asymmetric central stalk (consisting primarily of the gamma subunit), causing it to rotate within the alpha3beta3 of F1 causing the 3 catalytic nucleotide binding sites to go through a series of conformational changes that leads to ATP synthesis. The major F1 subunits are prevented from rotating in sympathy with the central stalk rotor by a peripheral stalk that joins the alpha3beta3 to the non-rotating portion of FO. The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F1 to FO. Under the right conditions, the enzyme reaction can also be carried out in reverse, with ATP hydrolysis driving proton pumping across the membrane.
The binding change mechanism involves the active site of a β subunit's cycling between three states.[11] In the "loose" state, ADP and phosphate enter the active site; in the adjacent diagram, this is shown in pink. The enzyme then undergoes a change in shape and forces these molecules together, with the active site in the resulting "tight" state (shown in red) binding the newly produced ATP molecule with very high affinity. Finally, the active site cycles back to the open state (orange), releasing ATP and binding more ADP and phosphate, ready for the next cycle of ATP production.[12]
Physiological role[edit]
Like other enzymes, the activity of F1FO ATP synthase is reversible. Large-enough quantities of ATP cause it to create a transmembrane proton gradient, this is used by fermenting bacteria that do not have an electron transport chain, but rather hydrolyze ATP to make a proton gradient, which they use to drive flagella and the transport of nutrients into the cell.
In respiring bacteria under physiological conditions, ATP synthase, in general, runs in the opposite direction, creating ATP while using the proton motive force created by the electron transport chain as a source of energy. The overall process of creating energy in this fashion is termed oxidative phosphorylation. The same process takes place in the mitochondria, where ATP synthase is located in the inner mitochondrial membrane and the F1-part projects into mitochondrial matrix. The consumption of ATP by ATP-synthase pumps proton cations into the matrix.
Evolution[edit]
The evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality.[13][14] This association appears to have occurred early in evolutionary history, because essentially the same structure and activity of ATP synthase enzymes are present in all kingdoms of life.[13] The F-ATP synthase displays high functional and mechanistic similarity to the V-ATPase.[15] However, whereas the F-ATP synthase generates ATP by utilising a proton gradient, the V-ATPase generates a proton gradient at the expense of ATP, generating pH values of as low as 1.[16]
The F1 region also shows significant similarity to hexameric DNA helicases, and the FO region shows some similarity to H+
-powered flagellar motor complexes.[15] The α3β3 hexamer of the F1 region shows significant structural similarity to hexameric DNA helicases; both form a ring with 3-fold rotational symmetry with a central pore. Both have roles dependent on the relative rotation of a macromolecule within the pore; the DNA helicases use the helical shape of DNA to drive their motion along the DNA molecule and to detect supercoiling, whereas the α3β3 hexamer uses the conformational changes through the rotation of the γ subunit to drive an enzymatic reaction.[17]
The H+
motor of the FO particle shows great functional similarity to the H+
motors that drive flagella.[15] Both feature a ring of many small alpha-helical proteins that rotate relative to nearby stationary proteins, using a H+
potential gradient as an energy source. This link is tenuous, however, as the overall structure of flagellar motors is far more complex than that of the FO particle and the ring with about 30 rotating proteins is far larger than the 10, 11, or 14 helical proteins in the FO complex.
The modular evolution theory for the origin of ATP synthase suggests that two subunits with independent function, a DNA helicase with ATPase activity and a H+
motor, were able to bind, and the rotation of the motor drove the ATPase activity of the helicase in reverse.[13][17] This complex then evolved greater efficiency and eventually developed into today's intricate ATP synthases. Alternatively, the DNA helicase/H+
motor complex may have had H+
pump activity with the ATPase activity of the helicase driving the H+
motor in reverse.[13] This may have evolved to carry out the reverse reaction and act as an ATP synthase.[14][18][19]
In different species[edit]
E. coli[edit]
E. coli ATP synthase is the simplest known form of ATP synthase, with 8 different subunit types.[20]
Yeast[edit]
Yeast ATP synthase is one of the best-studied eukaryotic ATP synthases; and five F1, eight FO subunits, and seven associated proteins have been identified.[7] Most of these proteins have homologues in other eukaryotes.[21][22][23]
Plant[edit]
In plants, ATP synthase is also present in chloroplasts (CF1FO-ATP synthase). The enzyme is integrated into thylakoid membrane; the CF1-part sticks into stroma, where dark reactions of photosynthesis (also called the light-independent reactions or the Calvin cycle) and ATP synthesis take place. The overall structure and the catalytic mechanism of the chloroplast ATP synthase are almost the same as those of the mitochondrial enzyme. However, in chloroplasts, the proton motive force is generated not by respiratory electron transport chain but by primary photosynthetic proteins.
Bovine[edit]
The ATP synthase isolated from bovine heart mitochondria (Bos taurus) is, in terms of biochemistry and structure, the best-characterized ATP synthase. Beef heart is used as a source for the enzyme because of the high concentration of mitochondria in cardiac muscle.[24][25][26]
Human[edit]
The following is a list of humans genes that encode components of ATP synthases:
ATP5A1, ATP5AL1
ATP5B, ATP5BL1
ATP5C2, ATP5D, ATP5E, ATP5F1, ATP5G1, ATP5G2, ATP5G3, ATP5H, ATP5HP1, ATP5I, ATP5J, ATP5J2, ATP5L, ATP5L2, ATP5O, ATP5S
ATP6, ATP6AP1, ATP6AP2
ATPSBL1, ATPSBL2
MT-ATP6, MT-ATP8
See also[edit]
ATP10 protein required for the assembly of the FO sector of the mitochondrial ATPase complex.
Chloroplast
Electron transfer chain
Flavoprotein
Mitochondrion
Oxidative phosphorylation
P-ATPase
Proton pump
Rotating locomotion in living systems
Transmembrane ATPase
V-ATPase
References[edit]
Jump up ^ Okuno D, Iino R, Noji H (April 2011). "Rotation and structure of FOF1-ATP synthase". Journal of Biochemistry. 149 (6): 655–64. doi:10.1093/jb/mvr049. PMID 21524994.
Jump up ^ Junge W, Nelson N (June 2015). "ATP synthase". Annual Review of Biochemistry. 84: 631–57. doi:10.1146/annurev-biochem-060614-034124. PMID 25839341.
Jump up ^ Kagawa Y, Racker E (May 1966). "Partial resolution of the enzymes catalyzing oxidative phosphorylation. 8. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase". The Journal of Biological Chemistry. 241 (10): 2461–6. PMID 4223640.
Jump up ^ Mccarty RE (November 1992). "A plant biochemist's view of H+
-ATPases and ATP synthases". The Journal of Experimental Biology. 172 (Pt 1): 431–441. PMID 9874753.
Jump up ^ PDB: 5ARA; Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL (October 2015). "Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM". eLife. 4: e10180. doi:10.7554/eLife.10180. PMC 4718723  . PMID 26439008.
Jump up ^ Goodsell D (December 2005). "ATP Synthase". Molecule of the Month. RCSB PDB. doi:10.2210/rcsb_pdb/mom_2005_12.
^ Jump up to: a b Velours J, Paumard P, Soubannier V, Spannagel C, Vaillier J, Arselin G, Graves PV (May 2000). "Organisation of the yeast ATP synthase F(0):a study based on cysteine mutants, thiol modification and cross-linking reagents". Biochimica et Biophysica Acta. 1458 (2–3): 443–56. doi:10.1016/S0005-2728(00)00093-1. PMID 10838057.
Jump up ^ Fernandez Moran H, Oda T, Blair PV, Green DE (July 1964). "A macromolecular repeating unit of mitochondrial structure and function. Correlated electron microscopic and biochemical studies of isolated mitochondria and submitochondrial particles of beef heart muscle". The Journal of Cell Biology. 22 (1): 63–100. doi:10.1083/jcb.22.1.63. PMC 2106494  . PMID 14195622.
Jump up ^ PDB: 1VZS; Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D (2004). "Solution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria". Journal of Molecular Biology. 342 (2): 593–603. doi:10.1016/j.jmb.2004.07.013. PMID 15327958.
Jump up ^ Guo H, Bueler SA, Rubinstein JL (Nov 2017). "Atomic model for the dimeric FO region of mitochondrial ATP synthase". Science. 358 (6365): 936–40. doi:10.1126/science.aao4815. PMID 29074581.
Jump up ^ Gresser MJ, Myers JA, Boyer PD (October 1982). "Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model". The Journal of Biological Chemistry. 257 (20): 12030–8. PMID 6214554.
Jump up ^ Nakamoto RK, Baylis Scanlon JA, Al-Shawi MK (August 2008). "The rotary mechanism of the ATP synthase". Archives of Biochemistry and Biophysics. 476 (1): 43–50. doi:10.1016/j.abb.2008.05.004. PMC 2581510  . PMID 18515057.
^ Jump up to: a b c d Doering C, Ermentrout B, Oster G (December 1995). "Rotary DNA motors". Biophysical Journal. 69 (6): 2256–67. Bibcode:1995BpJ....69.2256D. doi:10.1016/S0006-3495(95)80096-2. PMC 1236464  . PMID 8599633.
^ Jump up to: a b Crofts A. "Lecture 10:ATP synthase". Life Sciences at the University of Illinois at Urbana-Champaign.
^ Jump up to: a b c "ATP Synthase". InterPro Database.
Jump up ^ Kim MS, Jang J, Ab Rahman NB, Pethe K, Berry EA, Huang LS (June 2015). "Isolation and Characterization of a Hybrid Respiratory Supercomplex Consisting of Mycobacterium tuberculosis Cytochrome bcc and Mycobacterium smegmatis Cytochrome aa3". The Journal of Biological Chemistry. 290 (23): 14350–60. doi:10.1074/jbc.m114.624312. PMC 4505504  . PMID 25861988.
^ Jump up to: a b Martinez LO, Jacquet S, Esteve JP, Rolland C, Cabezón E, Champagne E, Pineau T, Georgeaud V, Walker JE, Tercé F, Collet X, Perret B, Barbaras R (January 2003). "Ectopic beta-chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis". Nature. 421 (6918): 75–9. Bibcode:2003Natur.421...75M. doi:10.1038/nature01250. PMID 12511957.
Jump up ^ Cross RL, Taiz L (January 1990). "Gene duplication as a means for altering H+/ATP ratios during the evolution of FOF1 ATPases and synthases". FEBS Letters. 259 (2): 227–9. doi:10.1016/0014-5793(90)80014-a. PMID 2136729.
Jump up ^ Cross RL, Müller V (October 2004). "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio". FEBS Letters. 576 (1–2): 1–4. doi:10.1016/j.febslet.2004.08.065. PMID 15473999.
Jump up ^ Ahmad Z, Okafor F, Laughlin TF. "Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase". Journal of Amino Acids. 2011: 785741. doi:10.4061/2011/785741. PMID 22312470.
Jump up ^ Devenish RJ, Prescott M, Roucou X, Nagley P (May 2000). "Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex". Biochimica et Biophysica Acta. 1458 (2–3): 428–42. doi:10.1016/S0005-2728(00)00092-X. PMID 10838056.
Jump up ^ Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM (November 2006). "Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase". The EMBO Journal. 25 (22): 5433–42. doi:10.1038/sj.emboj.7601410. PMID 17082766.
Jump up ^ Stock D, Leslie AG, Walker JE (November 1999). "Molecular architecture of the rotary motor in ATP synthase". Science. 286 (5445): 1700–5. PMID 10576729.
Jump up ^ Abrahams JP, Leslie AG, Lutter R, Walker JE (August 1994). "Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria". Nature. 370 (6491): 621–8. doi:10.1038/370621a0. PMID 8065448.
Jump up ^ Gibbons C, Montgomery MG, Leslie AG, Walker JE (November 2000). "The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution". Nature Structural Biology. 7 (11): 1055–61. doi:10.1038/80981. PMID 11062563.
Jump up ^ Menz RI, Walker JE, Leslie AG (August 2001). "Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis". Cell. 106 (3): 331–41. PMID 11509182.
Further reading[edit]
Nick Lane: The Vital Question - Energy, Evolution, and the Origins of Complex Life, Ww Norton, 2015-07-20, ISBN 978-0393088816 (Link points to Figure 10 showing model of ATP synthase)
External links[edit]
Boris A. Feniouk: "ATP synthase — a splendid molecular machine"
Well illustrated ATP synthase lecture by Antony Crofts of the University of Illinois at Urbana-Champaign.
Proton and Sodium translocating F-type, V-type and A-type ATPases in OPM database
The Nobel Prize in Chemistry 1997 to Paul D. Boyer and John E. Walker for the enzymatic mechanism of synthesis of ATP; and to Jens C. Skou, for discovery of an ion-transporting enzyme, Na+
, K+
-ATPase.
Harvard Multimedia Production Site — Videos — ATP synthesis animation
David Goodsell: "ATP Synthase- Molecule of the Month"
[show]
v
t
e
Membrane transport protein: ion pumps, ATPases / ATP synthase (TC 3A2-3A3)
F-, V-, and A-type ATPase (3.A.2)
H+ (F-type)
H+ transporting, mitochondrial: ATP5A1
ATP5B
ATP5C1
ATP5C2
ATP5D
ATP5E
ATP5F1
ATP5G1
ATP5G2
ATP5G3
ATP5H
ATP5I
ATP5J
ATP5J2
ATP5L
ATP5L2
ATP5O
ATP5S
H+ (V-type)
H+ transporting, lysosomal: ATP6AP1
ATP6AP2
ATP6V1A
ATP6V1B1
ATP6V1B2
ATP6V1C1
ATP6V1C2
ATP6V1D
ATP6V1E1
ATP6V1E2
ATP6V1F
ATP6V1G1
ATP6V1G2
ATP6V1G3
ATP6V1H
ATP6V0A1
ATP6V0A2
ATP6V0A4
ATP6V0B
ATP6V0C
ATP6V0D1
ATP6V0D2
ATP6V0E
ATP6V0E1
TCIRG1
A-ATPase
found in Archea
P-type ATPase (3.A.3)
3.A.3.1.1: Na+/K+ transporting: ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
ATP1G1
3.A.3.1.2: H+/K+
H+/K+ exchanging: ATP4A
ATP4B
3.A.3.1.4: H+/K+ transporting, nongastric: ATP12A
3.A.3.2: Ca2+ (SERCA, PMCA, SPCA) / Ca2+ transporting: ATP2A1
ATP2A2
ATP2A3
ATP2B1
ATP2B2
ATP2B3
ATP2B4
ATP2C1
3.A.3.5: Cu2+ transporting: ATP7A
ATP7B
3.A.3.8.8: flippase: ATP8A2
Other/ungrouped:
Na+/K+ – H+
Mg2+ transporting: ATP3
Class I, type 8: ATP8A1
ATP8B1
ATP8B2
ATP8B3
ATP8B4
Class II, type 9: ATP9A
ATP9B
Class V, type 10: ATP10A
ATP10B
ATP10D
Class VI, type 11: ATP11A
ATP11B
ATP11C
type 13: ATP13A1
ATP13A2
ATP13A3
ATP13A4
ATP13A5
see also ATPase disorders
[show]
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Mitochondrial proteins
Outer membrane
fatty acid degradation
Carnitine palmitoyltransferase I
Long-chain-fatty-acid—CoA ligase
tryptophan metabolism
Kynureninase
monoamine neurotransmitter
metabolism
Monoamine oxidase
Intermembrane space
Adenylate kinase
Creatine kinase
Inner membrane
oxidative phosphorylation
Coenzyme Q – cytochrome c reductase
Cytochrome c
NADH dehydrogenase
Succinate dehydrogenase
pyrimidine metabolism
Dihydroorotate dehydrogenase
mitochondrial shuttle
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other
Glutamate aspartate transporter
Glycerol-3-phosphate dehydrogenase
ATP synthase
Carnitine palmitoyltransferase II
Uncoupling protein
Matrix
citric acid cycle
Citrate synthase
Aconitase
Isocitrate dehydrogenase
Oxoglutarate dehydrogenase complex
Succinyl coenzyme A synthetase
Fumarase
Malate dehydrogenase
anaplerotic reactions
Aspartate transaminase
Glutamate dehydrogenase
Pyruvate dehydrogenase complex
urea cycle
Carbamoyl phosphate synthetase I
Ornithine transcarbamylase
N-Acetylglutamate synthase
alcohol metabolism
ALDH2
PMPCB
Other/to be sorted
steroidogenesis
Cholesterol side-chain cleavage enzyme
Steroid 11-beta-hydroxylase
Aldosterone synthase
Frataxin
Mitochondrial membrane transport protein
Mitochondrial permeability transition pore
Mitochondrial carrier
Mitochondrial DNA
Complex I
MT-ND1
MT-ND2
MT-ND3
MT-ND4
MT-ND4L
MT-ND5
MT-ND6
Complex III
MT-CYB
Complex IV
MT-CO1
MT-CO2
MT-CO3
ATP synthase
MT-ATP6
MT-ATP8
tRNA
MT-TA
MT-TC
MT-TD
MT-TE
MT-TF
MT-TG
MT-TH
MT-TI
MT-TK
MT-TL1
MT-TL2
MT-TM
MT-TN
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MT-TQ
MT-TR
MT-TS1
MT-TS2
MT-TT
MT-TV
MT-TW
MT-TY
see also mitochondrial diseases
[show]
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Hydrolases: acid anhydride hydrolases (EC 3.6)
3.6.1
Pyrophosphatase
Inorganic
Thiamine
Apyrase
Thiamine-triphosphatase
3.6.2
Adenylylsulfatase
Phosphoadenylylsulfatase
3.6.3-4: ATPase
3.6.3
Cu++ (3.6.3.4)
Menkes/ATP7A
Wilson/ATP7B
Ca+ (3.6.3.8)
SERCA
ATP2A1
ATP2A2
ATP2A3
Plasma membrane
ATP2B1
ATP2B2
ATP2B3
ATP2B4
SPCA
ATP2C1
ATP2C2
Na+/K+ (3.6.3.9)
ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
H+/K+ (3.6.3.10)
ATP4A
Other P-type ATPase
ATP8B1
ATP10A
ATP11B
ATP12A
ATP13A2
ATP13A3
3.6.4
Dynein
Kinesin
Myosin
Katanin
3.6.5: GTPase
3.6.5.1: Heterotrimeric G protein
Gαs
Gαi
GNAI1
GNAI2
GNAI3
Gαq/11
GNAQ
GNA11
Gα12/13
GNA12
GNA13
Transducin
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GNAT3
3.6.5.2: Small GTPase > Ras superfamily
Rho family of GTPases: Cdc42
CDC42
TC10
TCL
RhoUV
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RhoV
Rac
Rac1
2
3
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RhoBTB
1
2
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Rho
A
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C
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1
2
3
RhoDF
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RhoD
other: Ras
HRAS
KRAS
NRAS
Rab
RAB23
RAB27
Arf
ARF6
SAR1B
ARL13B
ARL6
Ran
Rheb
Rap
RGK
3.6.5.3: Protein-synthesizing GTPase
Prokaryotic
IF-2
EF-Tu
EF-G
Eukaryotic
3.6.5.5-6: Polymerization motors
Dynamin
Tubulin
[show]
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Enzyme inhibitor
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EC number
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List of enzymes
Kinetics
Enzyme kinetics
Eadie–Hofstee diagram
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Types
EC1 Oxidoreductases (list)
EC2 Transferases (list)
EC3 Hydrolases (list)
EC4 Lyases (list)
EC5 Isomerases (list)
EC6 Ligases (list)
Molecular and Cellular Biology portal
Retrieved from "https://en.wikipedia.org/w/index.php?title=ATP_synthase&oldid=821081799"
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value: АТФ синтаза – Bulgarian

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value: ای‌تی‌پی سنتاز – Persian

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value: ATPasi trasportante H+ tra due settori – Italian

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value: H+ transportujuća dvosektorna ATPaza – Serbian

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