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
Date Published1994 Dec
KeywordsAmino Acid Sequence, Animals, Catalysis, Chloroplasts, Down-Regulation, Mitochondria, Molecular Sequence Data, Proton-Translocating ATPases

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.

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