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Mutational analysis of F1F0 ATPase: catalysis and energy coupling.

作者信息

Omote H, Futai M

机构信息

Division of Biological Sciences, Osaka University, Ibaraki, Japan.

出版信息

Acta Physiol Scand Suppl. 1998 Aug;643:177-83.

PMID:9789559
Abstract

Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Extensive mutational analyses identified essential residues for catalysis and conformation transmission. Pseudorevertant studies revealed that beta/alpha and beta/gamma subunits interactions are important for the energy coupling between catalysis and H+ translocation. In this article, we discuss mechanism of catalysis and energy coupling based on our recent mutation studies.

摘要

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Mutational analysis of F1F0 ATPase: catalysis and energy coupling.
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