ATP synthesis catalyzed by the mitochondrial F1-F0 ATP synthase is not a reversal of its ATPase activity.

Abstract:

:The ADP(Mg2+)-deactivated oligomycin-sensitive F1-F0 ATPase of coupled submitochondrial particles treated with the substoichiometric amount of oligomycin was studied to test whether ATP synthesis and hydrolysis proceed in either direction through the same intermediates. The initial rates of ATP hydrolysis, oxidative phosphorylation, ATP-dependent, succinate-supported NAD+ reduction, and ATP-induced delta microH+ generation were measured using deactivated ATPase trapped by azide [Biochem. J. (1982) 202, 15-23]. Three ATP consuming reactions were strongly inhibited when azide was present in the assay mixtures, whereas ATP synthesis was not altered by azide. The unidirectional effect of azide is not consistent with three alternating binding sites mechanism operating in ATP synthesis and support our hypothesis on the existence of nucleotide(Mg2+)-controlled 'synthase' and 'hydrolase' states of the mitochondrial F1-F0 ATPase.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Syroeshkin AV,Vasilyeva EA,Vinogradov AD

doi

10.1016/0014-5793(95)00487-t

subject

Has Abstract

pub_date

1995-06-05 00:00:00

pages

29-32

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00487-T

journal_volume

366

pub_type

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