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Structure and mechanism of proton‐translocating transhydrogenase
Author(s) -
Jackson J.Baz,
Peake Sarah J.,
White Scott A.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01644-0
Subject(s) - chemistry , nad+ kinase , transmembrane protein , crystal structure , biophysics , affinities , oxidoreductase , binding site , stereochemistry , proton , crystallography , biochemistry , enzyme , biology , receptor , physics , quantum mechanics
Recent developments have led to advances in our understanding of the structure and mechanism of action of proton‐translocating (or AB ) transhydrogenase. There is (a) a high‐resolution crystal structure, and an NMR structure, of the NADP(H)‐binding component (dIII), (b) a homology‐based model of the NAD(H)‐binding component (dI) and (c) an emerging consensus on the position of the transmembrane helices (in dII). The crystal structure of dIII, in particular, provides new insights into the mechanism by which the energy released in proton translocation across the membrane is coupled to changes in the binding affinities of NADP + and NADPH that drive the chemical reaction.