|Title||The regulation of catalysis in ATP synthase.|
|Publication Type||Journal Article|
|Year of Publication||1994|
|Journal||Curr Opin Struct Biol|
|Date Published||1994 Dec|
|Keywords||Amino 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 Journal||Curr. Opin. Struct. Biol.|