Premium
The γ subunit of F 1 and the PVP protein of F o (F o I) are components of the gate of the mitochondrial F o F 1 H + ‐ATP synthase
Author(s) -
Papa S.,
Guerrieri F.,
Zanotti F.,
Fiermonte M.,
Capozza G.,
Jirillo E.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80462-r
Subject(s) - protein subunit , dithiothreitol , reagent , chemistry , moiety , atp synthase , bifunctional , mitochondrion , transmembrane protein , biochemistry , stereochemistry , enzyme , receptor , gene , catalysis
The γ subunit of the F 1 moiety of the bovine mitochondrial H + ‐ATP synthase is shown to function as a component of the gate. Addition of purified γ subunit to F o ‐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 γ subunit with the PVP protein of the F o sector.