The regulation of catalysis in ATP synthase.

TitleThe regulation of catalysis in ATP synthase.
Publication TypeJournal Article
Year of Publication1994
AuthorsWalker, JE
JournalCurr Opin Struct Biol
Volume4
Issue6
Pagination912-8
Date Published1994 Dec
ISSN0959-440X
KeywordsAmino Acid Sequence, Animals, Catalysis, Chloroplasts, Down-Regulation, Mitochondria, Molecular Sequence Data, Proton-Translocating ATPases
Abstract

ATP synthase is regulated so as to prevent futile hydrolysis of ATP when the transmembrane proton electrochemical gradient, delta mu H+, falls. Mitochondria and chloroplasts have different mechanisms for inhibition of ATP synthase: by binding an inhibitor protein, and by stabilization of the ADP-inhibited state by making an intramolecular disulphide bond, respectively. The recently determined structure of bovine F1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.

DOI10.1016/0959-440X(94)90274-7
Alternate JournalCurr. Opin. Struct. Biol.
Citation Key10.1016/0959-440X(94)90274-7
PubMed ID7712295