Purification and characterization of sulfur reductase from a moderately thermophilic bacterial strain, TI-1, that oxidizes iron.

@article{Sugio1998PurificationAC,
  title={Purification and characterization of sulfur reductase from a moderately thermophilic bacterial strain, TI-1, that oxidizes iron.},
  author={T. Sugio and K. Oda and K. Matsumoto and M. Takai and S. Wakasa and K. Kamimura},
  journal={Bioscience, biotechnology, and biochemistry},
  year={1998},
  volume={62 4},
  pages={
          705-9
        }
}
A moderately thermophilic bacterium, strain TI-1, produces H2S outside of the cells when grown at 45 degrees C on Fe(2+)-medium (pH 1.8) containing elemental sulfur and L-glutamic acid. A newly identified sulfur reductase was present in the cytosol of this strain and was purified to an electrophoretically homogeneous state from strain TI-1. The apparent molecular weight of sulfur reductase was 86,000 by gel filtration and 48,000 by SDS-PAGE, so the enzyme was a homodimer. The enzyme was most… Expand
DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

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