Energy transfer between the nicotinamide nucleotide transhydrogenase and ATP synthase of Escherichia coli.

ABSTRACT: Membrane bound nicotinamide nucleotide transhydrogenase (TH) catalyses the hydride transfer from NADH to NADP⁺. Under physiological conditions, this reaction is endergonic and must be energized by the pmf, coupled to transmembrane proton transport. Recent structures of transhydrogenase holoenzymes suggest new mechanistic details, how the long-distance coupling between hydride transfer in the peripheral nucleotide binding sites and the membrane-localized proton transfer occurs that now must be tested experimentally. Here, we provide protocols for the efficient expression and purification of the Escherichia coli transhydrogenase and its reconstitution into liposomes, alone or together with the Escherichia coli F₁F₀ ATP synthase. We show that E. coli transhydr

SUBMITTER: Graf SS 

PROVIDER: S-EPMC8551311 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature