Evidence for a nucleotide binding site on the isolated .beta. subunit from Escherichia coli F1-ATPase. Interaction between nucleotide and aurovertin D binding sites
- 18 December 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (26), 6591-6595
- https://doi.org/10.1021/bi00321a048
Abstract
The nucleotide binding capacity and affinity of the isolated .beta. subunit from Escherichia coli F1-ATPase were studied with radiolabeled ADP and ATP by an equilibrium dialysis technique. Each mole of .beta. subunit in the presence of EDTA bound 1 mol of ADP or ATP with Kd values of 25 .mu.M and 50-100 .mu.M, respectively. At a saturating concentration, aurovertin enhanced the affinity of ADP or ATP for the isolated .beta. subunit by 3- to 6-fold. The Kd values for the binding of ADP or ATP were also assessed through the enhancing effect of ADP on [14C]aurovertin binding; the Kd values determined by this approach were several times lower than in the absence of aurovertin, in agreement with results obtained by direct titration with radiolabeled ADP or ATP.Keywords
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