@article {5225,
	title = {Reaction of human myoglobin and nitric oxide - Heme iron or protein sulfhydryl (S) nitrosation dependence on the absence or presence of oxygen},
	journal = {Journal of Biological Chemistry},
	volume = {276},
	number = {6},
	year = {2001},
	note = {ISI Document Delivery No.: 401HBTimes Cited: 33Cited Reference Count: 58},
	month = {Feb},
	pages = {3991-3998},
	type = {Article},
	abstract = {The amino acid sequence of human myoglobin (Mb) is similar to other mammalian Mb except for a unique cysteine residue at position 110 (Cys(110)). Anaerobic treatment of ferrous forms of wild-type human Rib, the C110A variant of human Mb or horse heart Mb, with either authentic NO or chemically derived NO in vitro yields heme-NO complexes as detected by electron paramagnetic resonance spectroscopy (EPR). By contrast, no EPR-detectable heme-NO complex was observed from the aerobic reactions of NO and either the ferric or oxy-Mb forms of wild-type human or horse heart myoglobins, Mass analyses of wild-type human Mb treated aerobically with NO indicated a mass increase of similar to 30 atomic mass units (i.e,, NO/Mb = 1 mol/mol), Mass analyses of the corresponding apoprotein after heme removal showed that NO was associated with the apoprotein fraction. New electronic maxima were detected at A(333) nm (epsilon = 3665 +/- 90 mol(-1) cm(-1); mean +/- S.D.) and A(545) nm (epsilon = 44 +/- 3 mol(-1) cm(-1)) in solutions of S-nitrosated wild-type human Mb (similar to S-nitrosoglutathione), Importantly, the sulfhydryl S-H stretch vibration for Cys(110) measured by Fourier transform infrared (nu similar to 2552 cm(-1)) was absent for both holo- and apo- forms of the wild-type human protein after aerobic treatment of the protein with NO. Together, these data indicate that the reaction of wild-type human Mb and NO yields either heme-NO or a novel S-nitrosated protein dependent on the oxidation state of the heme iron and the presence or absence of dioxygen.},
	keywords = {ELECTRON-SPIN-RESONANCE, GLUTATHIONE, HEMOGLOBIN, HUMAN SKELETAL-MUSCLE, METMYOGLOBIN, NITROSOTHIOLS, OXIDATION, RELAXING FACTOR, SMOOTH-MUSCLE, VASCULAR TONE},
	isbn = {0021-9258},
	url = {<Go to ISI>://000166921200038},
	author = {Witting, P. K. and Douglas, D. J. and Mauk, A. G.}
}
