Zooming in on ATP hydrolysis in F1

Markus Dittrich; Klaus Schulten

doi:10.1007/s10863-005-9487-7

Zooming in on ATP hydrolysis in F₁

Markus Dittrich, Klaus Schulten

Research output: Contribution to journal › Review article › peer-review

Abstract

We summarize our current view of the reaction mechanism in F ₁-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F₁ takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay mechanism. The chemical reaction itself is controlled by the spatial position of a key arginine residue.

Original language	English (US)
Pages (from-to)	441-444
Number of pages	4
Journal	Journal of Bioenergetics and Biomembranes
Volume	37
Issue number	6
DOIs	https://doi.org/10.1007/s10863-005-9487-7
State	Published - Dec 2005
Externally published	Yes

Keywords

ATP
F1-ATPase
Hydrolysis
Molecular mechanics
QM/MM

ASJC Scopus subject areas

Physiology
Cell Biology

Online availability

10.1007/s10863-005-9487-7

Library availability

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Cite this

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title = "Zooming in on ATP hydrolysis in F1",

abstract = "We summarize our current view of the reaction mechanism in F 1-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F1 takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay mechanism. The chemical reaction itself is controlled by the spatial position of a key arginine residue.",

keywords = "ATP, F1-ATPase, Hydrolysis, Molecular mechanics, QM/MM",

author = "Markus Dittrich and Klaus Schulten",

note = "Funding Information: This work is supported by grants from the National Institutes of Health grant no. PHS-5-P41-RR05969 and the National Science Foundation grant no. MCB02-34938. The authors gladly acknowledge supercomputer time provided by Pittsburgh Supercomputer Center and the National Center for Supercomputing Applications via National Resources Allocation Committee grant MCA93S028.",

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pages = "441--444",

journal = "Journal of Bioenergetics and Biomembranes",

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AU - Dittrich, Markus

AU - Schulten, Klaus

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PY - 2005/12

Y1 - 2005/12

N2 - We summarize our current view of the reaction mechanism in F 1-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F1 takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay mechanism. The chemical reaction itself is controlled by the spatial position of a key arginine residue.

AB - We summarize our current view of the reaction mechanism in F 1-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F1 takes place without the release of any significant free energy and is efficiently driven by the combined action of two water molecules utilizing a so-called protein-relay mechanism. The chemical reaction itself is controlled by the spatial position of a key arginine residue.

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KW - F1-ATPase

KW - Hydrolysis

KW - Molecular mechanics

KW - QM/MM

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