Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties.

@article{Bizouarn2000ProtonTN,
  title={Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties.},
  author={Tania Bizouarn and Ola Fjellstr{\"o}m and J Meuller and Magnus Axelsson and Anders Bergkvist and Carina Johansson and B G{\"o}ran Karlsson and Jan Rydstr{\"o}m},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1457 3},
  pages={211-28}
}
Transhydrogenase couples the stereospecific and reversible transfer of hydride equivalents from NADH to NADP(+) to the translocation of proton across the inner membrane in mitochondria and the cytoplasmic membrane in bacteria. Like all transhydrogenases, the Escherichia coli enzyme is composed of three domains. Domains I and III protrude from the membrane and contain the binding site for NAD(H) and NADP(H), respectively. Domain II spans the membrane and constitutes at least partly the proton… CONTINUE READING

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