| Literature DB >> 2172010 |
S Papa1, F Guerrieri, F Zanotti, M Fiermonte, G Capozza, E Jirillo.
Abstract
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.Entities:
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Year: 1990 PMID: 2172010 DOI: 10.1016/0014-5793(90)80462-r
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124