The highly conserved Glu149 and Tyr190 residues contribute to peroxynitrite-mediated nitrotyrosine formation and the catalytic activity of cytochrome P450 2B1

Chemical Research in Toxicology

Volumn 18, Issue 8, 2005, Pages 1203-1210

  Lin, Hsia Lien ^a   Zhang, Haoming ^b   Waskell, Lucy ^b   Hollenberg, Paul F ^a,c  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 NITROTYROSINE; ALANINE; BENZYL DERIVATIVE; CYTOCHROME P450; CYTOCHROME P450 2B1; GLUTAMIC ACID; HYDROXYL GROUP; MUTANT PROTEIN; OXIDOREDUCTASE; PEROXYNITRITE; PHENYLALANINE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STRUCTURE; GENE MUTATION; HYDROGEN BOND; MODEL; NITRATION; NONHUMAN; PROTEIN FUNCTION; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; WILD TYPE;

CATALYSIS; CONSERVED SEQUENCE; CYTOCHROME P-450 CYP2B1; ESCHERICHIA COLI; GLUTAMINE; HEME; HYDROGEN BONDING; IRON; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PEROXYNITROUS ACID; PLASMIDS; TEMPERATURE; TYROSINE;

EID: 23844555866     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx050100o     Document Type: Article

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