Báo cáo Y học: The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F1-ATPase
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F1-ATPase is inactivated by entrapment of MgADP in catalytic sites and reactivatedbyMgATPorPi.Here, usinga mutant a3b3c complex of thermophilic F1-ATPase (aW463F/bY341W) and monitoring nucleotide binding by ¯uorescence quenching of an introduced tryptophan, we found that P i interfered with the binding of MgATP to F1-ATPase, but binding ofMgADPwas interferedwith to a lesser extent.
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