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 Lettjournal_title
FEBS lettersauthors
Syroeshkin AV,Vasilyeva EA,Vinogradov ADdoi
10.1016/0014-5793(95)00487-tsubject
Has Abstractpub_date
1995-06-05 00:00:00pages
29-32issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(95)00487-Tjournal_volume
366pub_type
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