Biochimica et Biophysica Acta 2015-01-01

Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.

Ségolène Laage, Yisong Tao, Ann E McDermott

Index: Biochim. Biophys. Acta 1848(1 Pt B) , 260-5, (2014)

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Abstract

The interaction of lipids with subunit c from F1F0 ATP synthase is studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interacts and copurifies with cardiolipin. Solid state NMR data on oligomeric rings of F0 show that the cardiolipin interacts with the c subunit in membrane bilayers. These studies offer strong support for the hypothesis that F0 has specific interactions with cardiolipin.Copyright © 2014. Published by Elsevier B.V.

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