Reconstitution of energy-linked activities of the solubilized F1F0 ATP synthase from Bacillus subtilis

Abstract

The F1F0 ATP synthases from wild-type Bacillus subtilis and an uncoupler-resistant mutant have comparable subunit structures. In accord with an earlier hypothesis, ATP hydrolysis and ATP-P(i) exchange by the two synthases were equally stimulated and inhibited by protonophores, respectively, when reconstituted alone in either wild-type or mutant lipids.