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-Pi exchange by the two synthases were equally stimulated and inhibited by protonophores, respectively, when reconstituted alone in either wild-type or mutant lipids.
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Hicks et al. (1994) studied this question.
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