Rubrerythrin

Rubrerythrin is a non-haem iron protein involved in oxidative stress tolerance in anaerobic bacteria.^[1] It contains a diiron site active site where peroxide is reduced to two water molecules and a mono-iron rubredoxin like domain thought to be involved in electron transfer.^[2]

References

^ "Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis". Mol Microbiol. 44: 479–88. Apr 2002. doi:10.1046/j.1365-2958.2002.02892.x. PMID 11972784.
^ "The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains". Nat Struct Biol. 3: 539–46. Jun 1996. doi:10.1038/nsb0696-539. PMID 8646540.

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[1] "Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis". Mol Microbiol. 44: 479–88. Apr 2002. doi:10.1046/j.1365-2958.2002.02892.x. PMID 11972784.

[2] "The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains". Nat Struct Biol. 3: 539–46. Jun 1996. doi:10.1038/nsb0696-539. PMID 8646540.

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