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J. Biol. Chem., Vol. 266, Issue 13, 8523-8530, 05, 1991

Differential additions to the myoglobin prosthetic heme group. Oxidative gamma-meso substitution by alkylhydrazines

YS Choe and PR Ortiz de Montellano
Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143-0446.

The oxidative reaction of equine myoglobin with alkylhydrazines results primarily in introduction of the alkyl group at the sterically hindered gamma-meso position. The gamma-meso adducts formed with ethyl- and n- butylhydrazine have been isolated and unambiguously identified. With high pressure liquid chromatography, evidence for the formation of similar adducts with methyl- and n-propylhydrazine but not tert-butyl-, 2,2,2-trifluoroethyl-, or 2-phenylethylhydrazine has also been obtained. The gamma regiospecificity of the reaction of myoglobin with alkylhydrazines contrasts with the delta meso regiospecificity in the alkylation of peroxidases. Addition to the porphyrin vinyl groups is not detected, but N-alkylheme adducts appear to be formed in very low yield. Cofactor studies establish that H2O2 is absolutely required for meso heme alkylation and EPR/spin trapping studies show that alkyl free radicals are the probable alkylating species. In contrast, the reductive reaction of sperm whale myoglobin with CBrCl3 results in addition of the CCl3.radical to the 2-vinyl moiety of the heme group (Osawa, Y., Highet, R. J., Murphy, C. M., Cotter. R.J., and Pohl, L.R. (1989) J. Am. Chem. Soc. 111, 4462-4467). Carbon radicals thus apparently add to different sites of the myoglobin prosthetic group under reductive and oxidative conditions, presumably because of differences in the oxidation state of the heme and/or the intrinsic reactivities of alkyl and polyhaloalkyl radicals.
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