@article {4978,
	title = {Reaction of human myoglobin and H2O2 - Involvement of a thiyl radical produced at cysteine 110},
	journal = {Journal of Biological Chemistry},
	volume = {275},
	number = {27},
	year = {2000},
	note = {ISI Document Delivery No.: 332QGTimes Cited: 55Cited Reference Count: 52},
	month = {Jul},
	pages = {20391-20398},
	type = {Article},
	abstract = {The human myoglobin (Mb) sequence is similar to other mammalian Mb sequences, except for a unique cysteine at position 110. Reaction of wild-type recombinant human Mb, the C110A variant of human Mb, or horse heart Mb with H2O2 (protein/H2O2 = 1:1.2 mol/mol) resulted in formation of tryptophan peroxyl (Trp-OO.) and tyrosine phenoxyl radicals as detected by EPR spectroscopy at 77 K. For wild-type human Mb, a second radical (g similar to 2.036) was detected after decay of Trp-OO. that was not observed for the C110A variant or horse heart Mb. When the spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) was included in the reaction mixture at protein/DMPO ratios less than or equal to 1:10 mol/mol, a DMPO adduct exhibiting broad absorptions was detected. Hyperfine couplings of this radical indicated a DMPO-thiyl radical. Incubation of mild-type human Mb with thiol-blocking reagents prior to reaction with peroxide inhibited DMPO adduct formation, whereas at protein/DMPO ratios greater than or equal to 1:25 mol/mol, DMPO-tyrosyl radical adducts were detected. Mass spectrometry of wild-type human Mb following reaction with H2O2 demonstrated the formation of a homodimer (mass of 34,107 +/- 5 atomic mass units) sensitive to reducing conditions. The human Mb C110A variant afforded no dimer under identical conditions. Together, these data indicate that reaction of wild-type human Mb and H2O2 differs from the corresponding reaction of other myoglobin species by formation of thiyl radicals that lead to a homodimer through intermolecular disulfide bond formation.},
	keywords = {ASCORBATE, CROSS-LINKING, enzyme catalysis, HEMOGLOBIN, HYDROGEN-PEROXIDE, LOW-DENSITY-LIPOPROTEIN, METMYOGLOBIN, OXIDATION, SPERM WHALE MYOGLOBIN, SPIN ADDUCTS},
	isbn = {0021-9258},
	url = {<Go to ISI>://000088084500025},
	author = {Witting, P. K. and Douglas, D. J. and Mauk, A. G.}
}
