Coupling H+ Transport And Atp Synthesis In F1Fo-Atp Synthases: Glimpses Of Interacting Parts In A Dynamic Molecular Machine
10.1242/jeb.200.2.217
Crossref journal-article
The Company of Biologists
Journal of Experimental Biology (237)
Abstract

ABSTRACT Reversible, F1Fo-type ATPases (also termed F-ATP synthases) catalyze the synthesis of ATP during oxidative phosphorylation. In animal cells, the enzyme traverses the inner mitochondrial membrane and uses the energy of an H+ electrochemical gradient, generated by electron transport, in coupling H+ translocation to ATP formation. Closely related enzymes are found in the plasma membrane of bacteria such as Escherichia coli, where the enzymes function reversibly depending upon nutritional circumstance. The F1Fo-type enzymes are more distantly related to a second family of H+-translocating ATPases, the vacuolar-type or V-ATPases. Recent structural information has provided important hints as to how these enzymes couple H+ transport to the chemical work of ATP synthesis. The simplest F1Fo-type enzymes, e.g. as in E. coli, are composed of eight types of subunits in an unusual stoichiometry of α3β3γδε (F1) and a1b2c12 (Fo). F1 extends from the membrane, with the α and β subunits alternating around a central subunit γ. ATP synthesis occurs alternately in different β subunits, the cooperative tight binding of ADP+Pi at one catalytic site being coupled to ATP release at a second. The differences in binding affinities appear to be caused by rotation of the γ subunit in the center of the α3β3 hexamer. The γ subunit traverses a 4.5 nm stalk connecting the catalytic subunits to the membrane-traversing Fo sector. Subunit c is the H+-translocating subunit of Fo. Protonation/deprotonation of Asp61 in the center of the membrane is coupled to structural changes in an extramembranous loop of subunit c which interacts with both the γ and ε subunits. Subunits γ and ε appear to move from one subunit c to another as ATP is synthesized. The torque of such movement is proposed to cause the rotation of γ within the α3β3 complex. Four protons are translocated for each ATP synthesized. The movement of γ and ε therefore probably involves a unit of four c subunits. The organization of subunits in Fo remains a mystery; it will have to be understood if we are to understand the mechanism of torque generation.

Bibliography

Fillingame, R. H. (1997). Coupling H+ Transport And Atp Synthesis In F1Fo-Atp Synthases: Glimpses Of Interacting Parts In A Dynamic Molecular Machine. Journal of Experimental Biology, 200(2), 217–224.

Authors 1
  1. Robert H. Fillingame (first)
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Dates
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Created 4 years, 4 months ago (April 25, 2021, 12:14 a.m.)
Deposited 1 year, 5 months ago (March 23, 2024, 7:11 p.m.)
Indexed 2 months ago (June 27, 2025, 6:40 a.m.)
Issued 28 years, 7 months ago (Jan. 15, 1997)
Published 28 years, 7 months ago (Jan. 15, 1997)
Published Online 28 years, 7 months ago (Jan. 15, 1997)
Published Print 28 years, 7 months ago (Jan. 15, 1997)
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@article{Fillingame_1997, title={Coupling H+ Transport And Atp Synthesis In F1Fo-Atp Synthases: Glimpses Of Interacting Parts In A Dynamic Molecular Machine}, volume={200}, ISSN={1477-9145}, url={http://dx.doi.org/10.1242/jeb.200.2.217}, DOI={10.1242/jeb.200.2.217}, number={2}, journal={Journal of Experimental Biology}, publisher={The Company of Biologists}, author={Fillingame, Robert H.}, year={1997}, month=jan, pages={217–224} }