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.
- Membrane-protein structure
- Nicotinamide nucleotide