title: Involvement of ATP synthase residues alphaArg-376, betaArg-182, and betaLys-155 in Pi binding.
abstract: alphaArg-376, betaLys-155, and betaArg-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 F(1)-ATPase that whereas Pi protected wild-type from reaction with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, mutations betaK155Q, betaR182Q, betaR182K, and alphaR376Q abolished protection. Therefore, in ATP synthesis initial binding of substrate Pi in open catalytic site betaE is supported by each of these three residues.
authors.affiliation: Department of Biochemistry and Biophysics, Box 712, University of Rochester Medical Center, Rochester, NY 14642, USA.
authors.forename: Zulfiqar
authors.initials: Z
authors.lastname: Ahmad
authors.forename: Alan E
authors.initials: AE
authors.lastname: Senior
mesh_terms: D009327:4-Chloro-7-nitrobenzofurazan / Q000037:antagonists & inhibitors / Q000494:pharmacology; D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000096:biosynthesis; D001120:Arginine / Q000737:chemistry* / Q000235:genetics; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites / Q000235:genetics; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D008239:Lysine / Q000737:chemistry* / Q000235:genetics; D017354:Point Mutation; D013379:Substrate Specificity
chemical_list: D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D001120:Arginine; D025243:Bacterial Proton-Translocating ATPases; D009327:4-Chloro-7-nitrobenzofurazan; D008239:Lysine