Abstract
Nucleotide binding to nucleotide-depleted F 1-ATPase from Escherichia coli (EcF 1) during MgATP hydrolysis in the presence of excess ɛ subunit has been studied using a combination of centrifugal filtration and column-centrifugation methods. The results show that nucleotide-binding properties of catalytic sites on EcF 1 are affected by the state of occupancy of noncatalytic sites. The ATP-concentration dependence of catalytic-site occupancy during MgATP hydrolysis demonstrates that a bi-site mechanism is responsible for the positive catalytic cooperativity observed during multi-site catalysis by EcF 1. The results suggest that a bi-site mechanism is a general feature of F 1 catalysis.
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