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

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

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)
174 Downloads (Pure)

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.
Original languageEnglish
Pages (from-to)2027-2033
Number of pages7
JournalFEBS Letters
Volume589
Issue number16
DOIs
Publication statusPublished - 1 Jul 2015

Keywords

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

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