ATP synthase - wikipedia ATP synthase 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 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / QuickGO show Search PMC articles PubMed articles NCBI proteins 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 all organisms. It is formed from adenosine diphosphate ( ADP ) and inorganic phosphate ( P ). The overall reaction catalyzed by ATP synthase is : ADP + P + H ⇌ ATP + H O + H The formation of ATP from ADP and P is energetically unfavorable and would normally proceed in the reverse direction. In order to drive this reaction forward, ATP synthase 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 ATP synthase 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, F and F, which has a rotational motor mechanism allowing for ATP production. Because of its rotating subunit ATP Synthase is a molecular machine. Contents 1 Nomenclature 2 Structure and function 2.1 F region 2.2 F 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 The F fraction derives its name from the term `` Fraction 1 '' and F ( 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 F unit of ATP synthase. These functional regions consist of different protein subunits -- refer to tables. This enzyme is used in synthesis of ATP through aerobic respiration. Structure and function Bovine mitochondrial ATP synthase. The F, F, axle, and stator regions are color coded magenta, green, orange, and cyan respectively. Simplified model of F F - 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 F and F. F causes rotation of F and is made of c - ring and subunits a, b, d, F6. F is made of α, β, γ, δ ( displaystyle alpha, \beta, gamma, delta ) subunits. F has a water - soluble part that can hydrolyze ATP. F on the other hand has mainly hydrophobic regions. F F creates a pathway for protons movement across the membrane. F region The F portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. This portion is located through the intermembrane space between the inter membrane space of the mitochondria. 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 F 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 through conformational changes, i.e. closed, half open and open states allows for ATP to be bound and released once synthesized. The F particle is large and can be seen in the transmission electron microscope by negative staining. These are particles of 9 nm diameter that pepper the inner mitochondrial membrane. F - Subunits Subunit Human Gene alpha ATP5A1, ATPAF2 beta ATP5B, ATPAF1, C16orf7 gamma ATP5C1 delta ATP5D epsilon ATP5E F region F subunit F6 from the peripheral stalk region of ATP synthase. Fo is a water insoluble protein with eight subunits and a transmembrane ring. The ring has a tetramer shape with a helix loop helix protein that goes though conformational changes when protonated and deprotonated, pushing neighboring subunits to rotate, causing the spinning of F which then also affects conformation of F, resulting in switching of states of alpha and beta subunits. The F 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 F region was determined by cryo - EM at an overall resolution of 3.6 Å This part of the enzyme is located inside the inter membrane space and is actually the portion that catalyzes the reaction between ADP and the inorganic phosphate. F - Main subunits Subunit Human Gene ATP6 ATP5F1 ATP5G1, ATP5G2, ATP5G3 Binding model Mechanism of ATP synthase. ADP and P ( 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 F 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 F 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 F region of ATP synthase. A portion of the F ( 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 alpha beta of F causing the 3 catalytic nucleotide binding sites to go through a series of conformational changes that lead to ATP synthesis. The major F subunits are prevented from rotating in sympathy with the central stalk rotor by a peripheral stalk that joins the alpha beta to the non-rotating portion of F. 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 F to F. 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. 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. Physiological role Like other enzymes, the activity of F F 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 F - part projects into mitochondrial matrix. The consumption of ATP by ATP - synthase pumps proton cations into the matrix. Evolution The evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality. 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. The F - ATP synthase displays high functional and mechanistic similarity to the V - ATPase. 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. The F region also shows significant similarity to hexameric DNA helicases, and the F region shows some similarity to H - powered flagellar motor complexes. The α β hexamer of the F 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 α β hexamer uses the conformational changes through the rotation of the γ subunit to drive an enzymatic reaction. The H motor of the F particle shows great functional similarity to the H motors that drive flagella. 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 F particle and the ring with about 30 rotating proteins is far larger than the 10, 11, or 14 helical proteins in the F 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. 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. This may have evolved to carry out the reverse reaction and act as an ATP synthase. In different species E coli E. coli ATP synthase is the simplest known form of ATP synthase, with 8 different subunit types. Yeast Yeast ATP synthase is one of the best - studied eukaryotic ATP synthases ; and five F, eight F subunits, and seven associated proteins have been identified. Most of these proteins have homologues in other eukaryotes. Plant In plants, ATP synthase is also present in chloroplasts ( CF F - ATP synthase ). The enzyme is integrated into thylakoid membrane ; the CF - 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 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. Human 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 ATP10 protein required for the assembly of the F 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 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 : 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. Bibcode : 2017Sci... 358... 936G. doi : 10.1126 / science. aao4815. PMID 29074581. Jump up ^ Gresser MJ, Myers JA, Boyer PD ( October 1982 ). `` Catalytic site cooperativity of beef heart mitochondrial F 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 : Doering C, Ermentrout B, Oster G ( December 1995 ). `` Rotary DNA motors ''. Biophysical Journal. 69 ( 6 ) : 2256 -- 67. Bibcode : 1995BpJ... 69.2256 D. doi : 10.1016 / S0006 - 3495 ( 95 ) 80096 - 2. PMC 1236464. PMID 8599633. ^ Jump up to : Crofts A. `` Lecture 10 : ATP synthase ''. Life Sciences at the University of Illinois at Urbana - Champaign. ^ Jump up to : `` ATP Synthase ''. InterPro Database. Jump up ^ Beyenbach, KW ; Wieczorek, H ( Feb 2006 ). `` The V - type H+ ATPase : molecular structure and function, physiological roles and regulation ''. J Exp Biol. 209 ( 4 ) : 577 -- 89. PMID 16449553. ^ Jump up to : 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 F F 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 ( 2011 ). `` Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase ''. Journal of Amino Acids. 2011 : 785741. doi : 10.4061 / 2011 / 785741. PMC 3268026. 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 F ATPase ''. The EMBO Journal. 25 ( 22 ) : 5433 -- 42. doi : 10.1038 / sj. emboj. 7601410. PMC 1636620. 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. doi : 10.1126 / science. 286.5445. 1700. 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. Bibcode : 1994Natur. 370... 621A. 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. doi : 10.1016 / s0092 - 8674 ( 01 ) 00452 - 4. PMID 11509182. Further reading 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 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 '' 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 : Ca ( SERCA, PMCA, SPCA ) / Ca transporting : ATP2A1 ATP2A2 ATP2A3 ATP2B1 ATP2B2 ATP2B3 ATP2B4 ATP2C1 3. A. 3.5 : Cu transporting : ATP7A ATP7B 3. A. 3.8. 8 : flippase : ATP8A2 Other / ungrouped : Na / K -- H Mg 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 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 Malate - aspartate shuttle Glycerol phosphate shuttle 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 MT - TP MT - TQ MT - TR MT - TS1 MT - TS2 MT - TT MT - TV MT - TW MT - TY see also mitochondrial diseases 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 GNAI1 GNAI2 GNAI3 GNAQ GNA11 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3 3.6. 5.2 : Small GTPase > Ras superfamily Rho family of GTPases : Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 RhoG RhoBTB RhoH Rho Rnd RhoDF RhoF 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 Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie -- Hofstee diagram Hanes -- Woolf plot Lineweaver -- Burk plot Michaelis -- Menten kinetics 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=847490919 '' Categories : Enzymes Cellular respiration Photosynthesis EC 3.6. 3 Integral membrane proteins Protein complexes Talk Search Contents About Wikipedia Български Bosanski Català Čeština Dansk Deutsch Español فارسی Français Galego 한국어 Հայերեն Bahasa Indonesia Italiano עברית Basa Jawa Bahasa Melayu 日本 語 Polski Português Русский Sardu Simple English Slovenčina Српски / srpski Srpskohrvatski / српскохрватски Basa Sunda Suomi Svenska Türkçe Українська Tiếng Việt 中文 25 more Edit links This page was last edited on 25 June 2018, at 18 : 47 ( UTC ). 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Question: where are atp synthase complexes located in plant cells
Answer: in chloroplasts