Involvement of ATP synthase residues aArg-376, bArg-182, and bLys-155 in Pi binding
نویسندگان
چکیده
aArg-376, bLys-155, and bArg-182 are catalytically important ATP synthase residues that were proposed to be involved in substrate Pi binding and subsequent steps of ATP synthesis [Senior, A.E., Nadanaciva, S. and Weber, J. (2002) Biochim. Biophys. Acta 1553, 188–211]. Here, it was shown using purified Escherichia coli F1-ATPase that whereas Pi protected wild-type from reaction with 7-chloro-4-nitrobenzo-2oxa-1,3-diazole, mutations bK155Q, bR182Q, bR182K, and aR376Q abolished protection. Therefore, in ATP synthesis initial binding of substrate Pi in open catalytic site bE is supported by each of these three residues. 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
منابع مشابه
Identification of phosphate binding residues of Escherichia coli ATP synthase.
Four positively-charged residues, namely betaLys-155, betaArg-182, betaArg-246, and alphaArg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site betaE where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of betaArg-246 is shown to be ...
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