Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli.

@article{Gon2001ElectronTA,
  title={Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli.},
  author={St{\'e}phanie Gon and Marie Th{\'e}r{\`e}se Giudici-Orticoni and Vincent M{\'e}jean and Chantal Iobbi-Nivol},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 15},
  pages={
          11545-51
        }
}
Reduction of trimethylamine N-oxide (E'(0(TMAO/TMA)) = +130 mV) in Escherichia coli is carried out by the Tor system, an electron transfer chain encoded by the torCAD operon and made up of the periplasmic terminal reductase TorA and the membrane-anchored pentahemic c-type cytochrome TorC. Although the role of TorA in the reduction of trimethylamine N-oxide (TMAO) has been clearly established, no direct evidence for TorC involvement has been presented. TorC belongs to the NirT/NapC c-type… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 30 CITATIONS

Microbial methylated amine metabolism in marine surface waters

VIEW 5 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Similar Papers