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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ahmad Z,Senior AE

doi

10.1016/j.febslet.2004.12.022

keywords:

subject

Has Abstract

pub_date

2005-01-17 00:00:00

pages

523-8

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(04)01557-1

journal_volume

579

pub_type

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