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Kinetic Analysis of ATPase Mechanisms

Published online by Cambridge University Press:  17 March 2009

D. R. Trentham ,
J. F. Eccleston  and
C. R. Bagshaw
D. R. Trentham
Affiliation:
Molecular Enzymology Laboratory, Department of Biochemistry, Medical School, University Walk, Bristol BS8 ITD, U. K.
J. F. Eccleston
Affiliation:
Molecular Enzymology Laboratory, Department of Biochemistry, Medical School, University Walk, Bristol BS8 ITD, U. K.
C. R. Bagshaw
Affiliation:
Molecular Enzymology Laboratory, Department of Biochemistry, Medical School, University Walk, Bristol BS8 ITD, U. K.
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Extract

At even the simplest level we can expect an ATPase mechanism to comprise the following four steps: the binding of ATP, the reaction of ATP with water on the enzyme, and the release of the products ADP and P1. So at the outset techniques are needed to investigate these four processes. The range of techniques needed is soon extended once questions are asked about the role of protons and metal ions, the possibility of a multistep hydrolytic process, multistep substrate and product binding processes, and protein–lipid or protein–protein interactions. Since ATPases and ATP synthases are almost universally involved in some form of energy transduction there is a particular need in an ATPase or ATP synthase reaction to evaluate the equilibrium constants of the steps in the mechanism and to investigate the possibility of alternate reaction pathways. The nature of the coupling process by the protein of the chemical reactions of ATP to the other energetic process, be it muscle contraction, active transport, respiration or photosynthesis, is likewise of profound interest. Finally we would like to know as much as possible about the ATPase or ATP synthase mechanism during the period when the various forms of energy transduction are occurring.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 9 , Issue 2 , May 1976 , pp. 217 - 281
Copyright
Copyright © Cambridge University Press 1976

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