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2010 - ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements

Icon N1   SURFE²R ONE (a predecessor model of SURFE²R N1) publication in FEBS Letters (2010)

Authors:
Tadini-Buoninsegni F., Bartolommei G., Moncelli M.R., Pilankatta R., Lewis D., Inesi G.

Journal:
FEBS Letters (2010) 584(22):4619-4622


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.


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