Download MendeleyThe high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria.
White, S.A., Peake, S.J., McSweeney, S., Leonard, G., Cotton, N.P., Jackson, J.B.(2000) Structure 8: 1-12
- PubMed: 10673423
- DOI: https://doi.org/10.1016/s0969-2126(00)00075-7
- Primary Citation of Related Structures:
1DJL - PubMed Abstract:
Transhydrogenase, located in the inner membranes of animal mitochondria and the cytoplasmic membranes of bacteria, couples the transfer of reducing equivalents between NAD(H) and NADP(H) to proton pumping. The protein comprises three subunits termed dI, dII and dIII. The dII component spans the membrane. The dI component, which contains the binding site for NAD(+)/NADH, and the dIII component, which has the binding site for NADP(+)/NADPH, protrude from the membrane. Proton pumping is probably coupled to changes in the binding affinities of dIII for NADP(+) and NADPH.
Organizational Affiliation:
School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK. s.a.white@bham.ac.uk
