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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response.

Sequence analyses of the Streptococcus faecalis NADH peroxidase and the flavoprotein component of the Salmonella typhimurium alkyl hydroperoxide reductase indicate clear evolutionary links with members of the flavoprotein disulfide reductase family. However, chemical and spectroscopic evidence demonstrate that the non-flavin redox center in NADH peroxidase is an unusual stabilized cysteine-sulfenic acid (Cys-SOH) derivative, and not a cystine disulfide as found in the disulfide reductases. This redox-active element, when appropriately stabilized by the respective protein environment, appears to play key roles in both the catalytic and regulatory aspects of the bacterial response to oxidative stress.[1]

References

  1. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Claiborne, A., Ross, R.P., Parsonage, D. Trends Biochem. Sci. (1992) [Pubmed]
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