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Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel
Author(s) -
Jackson J. Baz,
Leung Josephine H.,
Stout Charles D.,
Schurig-Briccio Lici A.,
Gennis Robert B.
Publication year - 2015
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/j.febslet.2015.06.027
Subject(s) - thermus thermophilus , gating , chemistry , enzyme , kinetics , redox , dimer , hexokinase , proton , biochemistry , biophysics , glycolysis , biology , physics , inorganic chemistry , organic chemistry , escherichia coli , quantum mechanics , gene
The membrane protein transhydrogenase in animal mitochondria and bacteria couples reduction of NADP + by NADH to proton translocation. Recent X‐ray data on Thermus thermophilus transhydrogenase indicate a significant difference in the orientations of the two dIII components of the enzyme dimer (Leung et al., 2015). The character of the orientation change, and a review of information on the kinetics and thermodynamics of transhydrogenase, indicate that dIII swivelling might assist in the control of proton gating by the redox state of bound NADP + /NADPH during enzyme turnover.