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ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements

Research Area: Uncategorized Year: 2010
Type of Publication: Article
Authors:
Journal: FEBS LETTERS Volume: 584
Number: 22 Pages: 4619-4622
Month: NOV 19
ISSN: 0014-5793
Abstract:
ATP7B is a copper dependent P-type ATPase, required for copper homeostasis. Taking advantage of high yield heterologous expression of recombinant protein, we investigated charge transfer in ATP7B. We detected charge displacement within a single catalytic cycle upon ATP addition and formation of phosphoenzyme intermediate. We attribute this charge displacement to movement of bound copper within ATP7B. Based on specific mutations, we demonstrate that enzyme activation by copper requires occupancy of a site in the N-terminus extension which is not present in other transport ATPases, as well as of a transmembrane site corresponding to the cation binding site of other ATPases. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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