Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

doi:10.1111/j.1432-1033.1995.478_2.x

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Article

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

European journal of biochemistry - 15 Oct 1995

Dmitriev O Y, Altendorf K, Fillingame R H

Abstract excerpt

Subunit c of the Escherichia coli F1F0-ATPase, purified in chloroform/methanol (2:1), was reconstituted with detergent-solubilized F0 subunits a and b to form a functionally active H+ channel. The rates of H+ uptake by the proteoliposomes containing the reconstituted F0 complex were comparable to...

Topics

Escherichia coli
Ion Transport
Mutation
Proton-Translocating ATPases
Protons

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