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Epsilon subunit of Escherichia coli F1-ATPase:...
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