Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution.

@article{Schneider1996CrystalSO,
  title={Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution.},
  author={Fr. Schneider and Jan-Thomas L{\"o}we and Robert Huber and Hermann Schindelin and Caroline Kisker and J{\"o}rg Kn{\"a}blein},
  journal={Journal of molecular biology},
  year={1996},
  volume={263 1},
  pages={
          53-69
        }
}
The periplasmic dimethyl sulfoxide reductase (DMSOR) from the photosynthetic purple bacterium Rhodobacter capsulatus functions as the terminal electron acceptor in its respiratory chain. The enzyme catalyzes the reduction of highly oxidized substrates like dimethyl sulfoxide to dimethyl sulfide. At a molybdenum redox center, two single electrons are transferred from cytochrome C556 to the substrate dimethyl sulfoxide, generating dimethyl sulfide and (with two protons) water. The enzyme was… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 21 extracted citations

Prokaryotic Systems Biology

Advances in Experimental Medicine and Biology • 2015

Similar Papers

Loading similar papers…