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Enzymes normally enhance the rates of biochemical reactions by preferentially binding and stabilizing the transition states rather than either the substrates or the products of a reaction. The F|-subunit of ATP synthase does not fit this norm so well as tight binding to ATP rather than a transition state is employed to make ATP. Explain the binding-change model of the mechanism of ATP-synthase. How and why is the proton-motive force used in the reaction cycle of ATP synthase

Enzymes normally enhance the rates of biochemical reactions by preferentially binding and stabilizing the transition states rather than either the substrates or the products of a reaction. The F|-subunit of ATP synthase does not fit this norm so well as tight binding to ATP rather than a transition state is employed to make ATP. Explain the binding-change model of the mechanism of ATP-synthase. How and why is the proton-motive force used in the reaction cycle of ATP synthase

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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Enzymes normally enhance the rates of biochemical reactions by preferentially binding and stabilizing the transition states rather than either the substrates or the products of a reaction. The F|-subunit of ATP synthase does not fit this norm so well as tight binding to ATP rather than a transition state is employed to make ATP. Explain the binding-change model of the mechanism of ATP-synthase. How and why is the proton-motive force used in the reaction cycle of ATP synthase?

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