Journal article
Epsilon subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis.
Abstract
The epsilon subunit of Escherichia coli F1-ATPase is a tightly bound but dissociable partial inhibitor of ATPase activity. The effects of epsilon on the enzyme were investigated by comparing the ATPase activity and aurovertin binding properties of the epsilon-depleted F1-ATPase and the epsilon-replete complex. Kinetic data of multisite ATP hydrolysis were analyzed to give the best fit for one, two, or three kinetic components. Each form of …
Authors
Dunn SD; Zadorozny VD; Tozer RG; Orr LE
Journal
Biochemistry, Vol. 26, No. 14, pp. 4488–4493
Publisher
American Chemical Society (ACS)
Publication Date
July 14, 1987
DOI
10.1021/bi00388a047
ISSN
0006-2960