The gamma subunit of F1 and the PVP protein of F0 (F0I) are components of the gate of the mitochondrial F0F1 H(+)-ATP synthase.
The gamma subunit of the F1 moiety of the bovine mitochondrial H(+)-ATP synthase is shown to function as a component of the gate. Addition of purified gamma subunit to F0-liposomes inhibits transmembrane proton conduction. This inhibition can be removed by the bifunctional thiol reagent diamide. Immunoblot analysis shows that the diamide effect is likely due to disulphide bridging of the gamma subunit with the PVP protein of the F0 sector.
Papa
S
S
Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.
Guerrieri
F
F
Zanotti
F
F
Fiermonte
M
M
Capozza
G
G
Jirillo
E
E
D000818:Animals; D002417:Cattle; D003958:Diamide / Q000494:pharmacology; D015151:Immunoblotting; D008081:Liposomes / Q000378:metabolism; D008929:Mitochondria, Heart / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D011522:Protons; D013329:Structure-Activity Relationship; D013367:Submitochondrial Particles / Q000201:enzymology*
D008081:Liposomes; D011522:Protons; D003958:Diamide; D006180:Proton-Translocating ATPases