Regular ArticleProtein Radicals in Myoglobin Dimerization and Myoglobin-Catalyzed Styrene Epoxidation☆
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Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: Evidence for peroxidatic activity and formation of protein-based radicals
2007, Journal of Biological ChemistryCitation Excerpt :These primary protein-based radicals may have then led, via internal electron transfer, to the formation of surface-exposed amino acid radical(s) with subsequent cross-linking of the protein. Such reactions have been observed in several hemeproteins, including sperm whale Mb, when reacted with H2O2 in the absence of an exogenous electron donor (37-43). In most cases reported to date, the process involves the formation of tyrosine-tyrosine cross-links.
Erythrocyte-derived epoxyeicosatrienoic acids
2007, Prostaglandins and Other Lipid MediatorsRed blood cells: Reservoirs of cis- and trans-epoxyeicosatrienoic acids
2005, Prostaglandins and Other Lipid MediatorsCatalase reaction by myoglobin mutants and native catalase: Mechanistic investigation by kinetic isotope effect
2004, Journal of Biological ChemistryCitation Excerpt :On the other hand, the distance in L29H/H64L Mb is too far from the heme iron (6.6 Å) to serve as the general acid-base catalyst (Fig. 6B) (10). Thus, the catalatic reaction of MLC and F43H/H64L Mb, in which the general acid-base catalyst is located at a proper position, could proceed via the ionic mechanism with a small KIE (<4) (Scheme 1A), whereas the other Mb mutants oxidize H2O2 via a mechanism that could be different from the ionic mechanism with exhibiting a large KIE (10–29) due to a lack of the general acid-base catalyst. Exclusive formation of 18O2 and 16O2 from a 50:50 mixture of H216O2 and H218O2 indicates that O2 is formed by two-electron oxidation of H2O2 without breaking the O-O bond.
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This work was supported by National Institutes of Health Grants DK30297 and GM32488.
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