Aqueous Access Pathways in ATP Synthase Subunit a: REACTIVITY OF CYSTEINE SUBSTITUTED INTO TRANSMEMBRANE HELICES 1, 3, AND 5

Subunit a is thought to play a key role in H⁺ transport-driven rotation of the subunit c ring in Escherichia coli F₁F₀ ATP synthase. In the membrane-traversing F₀ sector of the enzyme, H⁺ binding and release occurs at Asp-61 in the middle of the second transmembrane helix (TMH) of subunit c. Protons...

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Veröffentlicht in:The Journal of biological chemistry 2007-03, Vol.282 (12), p.9001-9007
Hauptverfasser: Angevine, Christine M, Herold, Kelly A.G, Vincent, Owen D, Fillingame, Robert H
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Sprache:eng
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