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

Research output: Contribution to journalArticlepeer-review


  • Baz Jackson
  • Josephine H. Leung
  • Charles D. Stout
  • Lici A. Schurig-briccio
  • Robert B. Gennis

Colleges, School and Institutes


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.


Original languageEnglish
Pages (from-to)2027-2033
Number of pages7
JournalFEBS Letters
Issue number16
Publication statusPublished - 1 Jul 2015


  • Transhydrogenase, Membrane-protein structure, Nicotinamide nucleotide, Proton-pump, Proton-gating