Format

Send to

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 2003 Jun 12;545(1):18-24.

Proton translocation by transhydrogenase.

Author information

1
School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. j.b.jackson@bham.ac.uk

Abstract

Transhydrogenase, in animal mitochondria and bacteria, couples hydride transfer between NADH and NADP(+) to proton translocation across a membrane. Within the protein, the redox reaction occurs at some distance from the proton translocation pathway and coupling is achieved through conformational changes. In an 'open' conformation of transhydrogenase, in which substrate nucleotides bind and product nucleotides dissociate, the dihydronicotinamide and nicotinamide rings are held apart to block hydride transfer; in an 'occluded' conformation, they are moved into apposition to permit the redox chemistry. In the two monomers of transhydrogenase, there is a reciprocating, out-of-phase alternation of these conformations during turnover.

PMID:
12788487
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center