Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel. Issue 16 (2nd July 2015)

• Record Type: Journal Article
• Authors: Jackson, J. Baz; Leung, Josephine H.; Stout, Charles D.; Schurig-Briccio, Lici A.; Gennis, Robert B.
• Is Part Of: FEBS letters. Volume 589:Issue 16(2015)
• Page Start: 2027
• Page End: 2033
• Publication Date: 2015-07-02
• Subjects: Transhydrogenase -- Membrane-protein structure -- Nicotinamide nucleotide -- Proton-pump -- Proton-gating; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.06.027
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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.