R I Grimley

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The Tyr residue in the mobile loop region of the soluble, domain I polypeptide (called Ths) of the proton-translocating transhydrogenase from Rhodospirillum rubrum has been substituted by Asn and by Phe. The recombinant proteins were expressed at high levels in Escherichia coli and purified to homogeneity. The two well defined resonances at 6.82 and(More)
Transhydrogenase from mitochondrial and bacterial membranes couples proton translocation to hydride transfer between NAD(H) and NADP(H). The enzyme has three domains, of which domains I and III protrude from the membrane. These possess the NAD(H)- and NADP(H)-binding sites, respectively, whereas domain II spans the membrane. In domain I there is a mobile(More)
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