Carbon-2 proton exchange at histidine-41 in bovine erythrocyte superoxide dismutase.
The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile. This residue is identified by tritiation, protein digestion and subsequent peptide 'mapping' as histidine-41. A half-life for the exchange of histidine C-2 1H for 2H in 2H2O as solvent, at pD 8.1 and 40 degrees C, is estimated as approx. 9.2h, by 1H nuclear-magnetic-resonance spectroscopy.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D004912:Erythrocytes / Q000201:enzymology; D006639:Histidine / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D011522:Protons; D013482:Superoxide Dismutase / Q000378:metabolism*
D000596:Amino Acids; D011522:Protons; D006639:Histidine; D013482:Superoxide Dismutase