Ontology highlight
ABSTRACT:
SUBMITTER: Molina-Heredia FP
PROVIDER: S-EPMC1595423 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Molina-Heredia Fernando P FP Houée-Levin Chantal C Berthomieu Catherine C Touati Danièle D Tremey Emilie E Favaudon Vincent V Adam Virgile V Nivière Vincent V
Proceedings of the National Academy of Sciences of the United States of America 20060925 40
The superoxide radical O(2)(-.) is a toxic by-product of oxygen metabolism. Two O(2)(-.) detoxifying enzymes have been described so far, superoxide dismutase and superoxide reductase (SOR), both forming H2O2 as a reaction product. Recently, the SOR active site, a ferrous iron in a [Fe(2+) (N-His)(4) (S-Cys)] pentacoordination, was shown to have the ability to form a complex with the organometallic compound ferrocyanide. Here, we have investigated in detail the reactivity of the SOR-ferrocyanide ...[more]