Thermodynamics of reverse electron transfer across site 1: ATP/2e- is greater than one.

Abstract:

:ATP-driven, rotenone-sensitive, reverse electron transfer from succinate to acetoacetate was measured in rat liver mitochondria in the presence of cyanide. In the approach to equilibrium, the absolute ratio of the free energy change of electron transfer to that of ATP hydrolysis exceeded 1, tending towards about 1 1/4. The data support an H+/2e- stoichiometry of 5 for Site 1 as predicted by a thirteen-proton model of chemiosmotic coupling.

authors

Freedman JA,Lemasters JJ

doi

10.1016/s0006-291x(84)80325-3

subject

Has Abstract

pub_date

1984-11-30 00:00:00

pages

8-13

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)80325-3

journal_volume

125

pub_type

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