An expanded mechanism for rhodanese catalysis.

@article{Schlesinger1974AnEM,
  title={An expanded mechanism for rhodanese catalysis.},
  author={Paul H Schlesinger and John W. Westley},
  journal={The Journal of biological chemistry},
  year={1974},
  volume={249 3},
  pages={780-8}
}
The kinetic behavior of rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) was investigated at pH values from 5.0 to 10.8. The binding of thiosulfate was shown to be dependent upon a pK’ of 9.9, with the protonated enzyme binding the substrate much more strongly than the deprotonated form. An enzymic nucleophile displaces sulfite to form the sulfur-substituted enzyme. This reaction was shown to be dependent upon a pK’ of 6.5, with the protonated form being unreactive. The sulfur… CONTINUE READING

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