Purification of Thiobacillus novellus sulfite oxidase. Evidence for the presence of heme and molybdenum.

@article{Toghrol1983PurificationOT,
  title={Purification of Thiobacillus novellus sulfite oxidase. Evidence for the presence of heme and molybdenum.},
  author={F Toghrol and William M. Southerland},
  journal={The Journal of biological chemistry},
  year={1983},
  volume={258 11},
  pages={6762-6}
}
Sulfite oxidase from Thiobacillus novellus has been purified 206-fold. The enzyme reduced both ferricyanide and cytochrome c. The ferricyanide activity was 3-5% of the cytochrome c activity. During purification, the absorbance ratio of A413 nm/A280 nm showed a continual increase, suggesting the presence of heme in the T. novellus sulfite oxidase molecule. The absorption spectrum of the enzyme is very similar to that of rat liver sulfite oxidase which contains cytochrome b5 type heme. Gel… CONTINUE READING
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