Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel | Zendy

Jackson J. Baz | Zendy; Leung Josephine H. | Zendy; Stout Charles D. | Zendy; Schurig-Briccio Lici A. | Zendy; Gennis Robert B. | Zendy

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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.

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