Notes on the mechanism of ATP synthesis

M. A. Bianchet; Peter L. Pedersen; L. Mario Amzel

doi:10.1023/A:1005673209883

Notes on the mechanism of ATP synthesis

M. A. Bianchet, Peter L. Pedersen, L. Mario Amzel

School of Medicine

Research output: Contribution to journal › Short survey › peer-review

17 Scopus citations

Abstract

The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and P_i assumes that all states of the F₁ portion of the ATP synthase have β subunits in "tight," "loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional β subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

Original language	English (US)
Pages (from-to)	517-521
Number of pages	5
Journal	Journal of Bioenergetics and Biomembranes
Volume	32
Issue number	5
DOIs	https://doi.org/10.1023/A:1005673209883
State	Published - 2000

Keywords

ATP synthesis
Conformational changes
F-ATPase

ASJC Scopus subject areas

Physiology
Cell Biology

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10.1023/A:1005673209883

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keywords = "ATP synthesis, Conformational changes, F-ATPase",

author = "Bianchet, {M. A.} and Pedersen, {Peter L.} and Amzel, {L. Mario}",

note = "Funding Information: Work referred to here on the rat liner F1 was supported by NIH grants GM 25432 (to L.M.A.) and CA10951 (to P.L.P.).",

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AU - Bianchet, M. A.

AU - Pedersen, Peter L.

AU - Amzel, L. Mario

N1 - Funding Information: Work referred to here on the rat liner F1 was supported by NIH grants GM 25432 (to L.M.A.) and CA10951 (to P.L.P.).

PY - 2000

Y1 - 2000

N2 - The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and Pi assumes that all states of the F1 portion of the ATP synthase have β subunits in "tight," "loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional β subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

AB - The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and Pi assumes that all states of the F1 portion of the ATP synthase have β subunits in "tight," "loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional β subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

KW - ATP synthesis

KW - Conformational changes

KW - F-ATPase

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JO - Journal of Bioenergetics and Biomembranes

JF - Journal of Bioenergetics and Biomembranes

IS - 5

ER -

Notes on the mechanism of ATP synthesis

Abstract

Keywords

ASJC Scopus subject areas

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