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

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

Biochimica et biophysica acta (2014-08-30)

Ségolène Laage, Yisong Tao, Ann E McDermott

ZUSAMMENFASSUNG

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.

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