Peroxidation of a specific tryptophan of metmyoglobin by hydrogen peroxide.
Globin-centered radicals at tyrosine and tryptophan residues and a peroxyl radical at an unknown location have been reported previously as products of the reaction of metmyoglobin with hydrogen peroxide. The peroxyl radical is shown here to be localized on tryptophan through the use of recombinant sperm whale myoglobin labeled with 13C at the indole ring C-3. Peroxyl radical formation was not prevented by site-directed mutations that replaced all three tyrosines, the distal histidine, or tryptophan 7 with non-oxidizable residues. In contrast, mutation of tryptophan 14 prevents peroxyl radical formation, implicating tryptophan 14 as the specific site of the peroxidation.
DeGray
J A
JA
Laboratory of Pharmacology and Chemistry, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA.
Gunther
M R
MR
Tschirret-Guth
R
R
Ortiz de Montellano
P R
PR
Mason
R P
RP
D000818:Animals; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D008786:Metmyoglobin / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D014364:Tryptophan / Q000378:metabolism*; D014907:Whales
D005609:Free Radicals; D008786:Metmyoglobin; D014364:Tryptophan; D006861:Hydrogen Peroxide