Editing ATP synthase (section)

== In different organisms ==
=== Bacteria ===
''{{vanchor|E. coli}}'' ATP synthase is the simplest known form of ATP synthase, with 8 different subunit types.<ref name=ecoli>{{cite journal | vauthors = Ahmad Z, Okafor F, Laughlin TF | title = Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase | journal = Journal of Amino Acids | volume = 2011 | pages = 785741 | year = 2011 | pmid = 22312470 | pmc = 3268026 | doi = 10.4061/2011/785741 | doi-access = free }}</ref>

Bacterial F-ATPases can occasionally operate in reverse, turning them into an ATPase.<ref name=pmid26671611>{{cite journal | vauthors = Kühlbrandt W, Davies KM | title = Rotary ATPases: A New Twist to an Ancient Machine | journal = Trends in Biochemical Sciences | volume = 41 | issue = 1 | pages = 106–116 | date = January 2016 | pmid = 26671611 | doi = 10.1016/j.tibs.2015.10.006 }}</ref> Some bacteria have no F-ATPase, using an A/V-type ATPase bidirectionally.<ref name=pmid24878343/>

=== Yeast ===
Yeast ATP synthase is one of the best-studied eukaryotic ATP synthases; and five F<sub>1</sub>, eight F<sub>O</sub> subunits, and seven associated proteins have been identified.<ref name="Velours_2000" /> Most of these proteins have homologues in other eukaryotes.<ref>{{cite journal | vauthors = Devenish RJ, Prescott M, Roucou X, Nagley P | title = Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex | journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics | volume = 1458 | issue = 2–3 | pages = 428–442 | date = May 2000 | pmid = 10838056 | doi = 10.1016/S0005-2728(00)00092-X | doi-access = free }}</ref><ref>{{cite journal | vauthors = Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM | title = Novel features of the rotary catalytic mechanism revealed in the structure of yeast F<sub>1</sub> ATPase | journal = The EMBO Journal | volume = 25 | issue = 22 | pages = 5433–5442 | date = November 2006 | pmid = 17082766 | pmc = 1636620 | doi = 10.1038/sj.emboj.7601410 }}</ref><ref>{{cite journal | vauthors = Stock D, Leslie AG, Walker JE | title = Molecular architecture of the rotary motor in ATP synthase | journal = Science | volume = 286 | issue = 5445 | pages = 1700–1705 | date = November 1999 | pmid = 10576729 | doi = 10.1126/science.286.5445.1700 }}</ref><ref>{{cite journal | vauthors = Liu S, Charlesworth TJ, Bason JV, Montgomery MG, Harbour ME, Fearnley IM, Walker JE | title = The purification and characterization of ATP synthase complexes from the mitochondria of four fungal species | journal = The Biochemical Journal | volume = 468 | issue = 1 | pages = 167–175 | date = May 2015 | pmid = 25759169 | pmc = 4422255 | doi = 10.1042/BJ20150197 }}</ref>

=== Plant ===
In plants, ATP synthase is also present in [[chloroplasts]] (CF<sub>1</sub>F<sub>O</sub>-ATP synthase). The enzyme is integrated into [[thylakoid]] membrane; the CF<sub>1</sub>-part sticks into [[stroma (fluid)|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 bacterial enzyme. However, in chloroplasts, the [[electrochemical potential|proton motive force]] is generated not by respiratory electron transport chain but by primary photosynthetic proteins. The synthase has a 40-aa insert in the gamma-subunit to inhibit wasteful activity when dark.<ref>{{cite journal | vauthors = Hahn A, Vonck J, Mills DJ, Meier T, Kühlbrandt W | title = Structure, mechanism, and regulation of the chloroplast ATP synthase | journal = Science | volume = 360 | issue = 6389 | pages = eaat4318 | date = May 2018 | pmid = 29748256 | pmc = 7116070 | doi = 10.1126/science.aat4318 | doi-access = free }}</ref>

=== Mammal ===
{{anchor|Bovine}}The ATP synthase isolated from bovine (''Bos taurus'') heart mitochondria 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. Their genes have close homology to human ATP synthases.<ref>{{cite journal | vauthors = Abrahams JP, Leslie AG, Lutter R, Walker JE | title = Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria | journal = Nature | volume = 370 | issue = 6491 | pages = 621–628 | date = August 1994 | pmid = 8065448 | doi = 10.1038/370621a0 | s2cid = 4275221 | bibcode = 1994Natur.370..621A }}</ref><ref>{{cite journal | vauthors = Gibbons C, Montgomery MG, Leslie AG, Walker JE | title = The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution | journal = Nature Structural Biology | volume = 7 | issue = 11 | pages = 1055–1061 | date = November 2000 | pmid = 11062563 | doi = 10.1038/80981 | s2cid = 23229994 }}</ref><ref>{{cite journal | vauthors = Menz RI, Walker JE, Leslie AG | title = Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis | journal = Cell | volume = 106 | issue = 3 | pages = 331–341 | date = August 2001 | pmid = 11509182 | doi = 10.1016/s0092-8674(01)00452-4 | s2cid = 1266814 | doi-access = free }}</ref>

{{anchor|Human}}Human genes that encode components of ATP synthases:
* ''[[ATP synthase, H+ transporting, mitochondrial F1 complex, alpha 1|ATP5A1]]''
* ''[[ATP5B]]''
* ''[[ATP5C1]]'', ''[[ATP5D]]'', ''[[ATP5E]]'', ''[[ATP5F1]]'', ''[[ATP5MC1]]'', ''[[ATP5G2]]'', ''[[ATP5G3]]'', ''[[ATP5H]]'', ''[[ATP5I]]'', ''[[ATP5J]]'', ''[[ATP5J2]]'', ''[[ATP5L]]'', ''[[ATP5O]]''
* ''[[MT-ATP6]]'', ''[[MT-ATP8]]''

=== Other eukaryotes ===
Eukaryotes belonging to some divergent lineages have very special organizations of the ATP synthase. A [[euglenozoa]] ATP synthase forms a dimer with a boomerang-shaped F<sub>1</sub> head like other mitochondrial ATP synthases, but the F<sub>O</sub> subcomplex has many unique subunits. It uses [[cardiolipin]]. The inhibitory IF<sub>1</sub> also binds differently, in a way shared with [[trypanosomatida]].<ref>{{cite journal | vauthors = Mühleip A, McComas SE, Amunts A | title = Structure of a mitochondrial ATP synthase with bound native cardiolipin | journal = eLife | volume = 8 | pages = e51179 | date = November 2019 | pmid = 31738165 | pmc = 6930080 | doi = 10.7554/eLife.51179 | doi-access = free }}
* {{cite web |date=December 24, 2019 |title=Different from the rest |website=eLife |url=https://elifesciences.org/digests/51179/different-from-the-rest}}</ref>

=== Archaea ===
Archaea do not generally have an F-ATPase. Instead, they synthesize ATP using the A-ATPase/synthase, a rotary machine structurally similar to the [[V-ATPase]] but mainly functioning as an ATP synthase.<ref name=pmid26671611/> Like the bacteria F-ATPase, it is believed to also function as an ATPase.<ref name=pmid24878343>{{cite journal | vauthors = Stewart AG, Laming EM, Sobti M, Stock D | title = Rotary ATPases--dynamic molecular machines | journal = Current Opinion in Structural Biology | volume = 25 | pages = 40–48 | date = April 2014 | pmid = 24878343 | doi = 10.1016/j.sbi.2013.11.013 | doi-access = free }}</ref>

=== LUCA and earlier ===

F-ATPase gene linkage and gene order are widely conserved across ancient prokaryote lineages, implying that this system already existed at a date before the [[last universal common ancestor]], the LUCA.<ref>{{cite journal | vauthors = Matzke NJ, Lin A, Stone M, Baker MA | title = Flagellar export apparatus and ATP synthetase: Homology evidenced by synteny predating the Last Universal Common Ancestor | journal = BioEssays | volume = 43 | issue = 7 | pages = e2100004 | date = July 2021 | pmid = 33998015 | doi = 10.1002/bies.202100004 | s2cid = 234747849 | hdl = 2292/55176 | hdl-access = free }}</ref>