Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis

Journal of Biological Chemistry

Volumn 275, Issue 17, 2000, Pages 12581-12589

  Gardner, Anne M ^a   Martin, Lori A ^a   Gardner, Paul R ^a   Dou, Yi ^b   Olson, John S ^b  

^a CINCINNATI CHILDREN'S HOSPITAL MEDICAL CENTER   (United States)

^b RICE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; HEME; HEMOGLOBIN DERIVATIVE; HYDROXYL GROUP; NITRATE; NITRIC OXIDE; OXYGENASE; PHENYLALANINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SCAVENGER; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ESCHERICHIA COLI; MICHAELIS CONSTANT; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; STEADY STATE;

AMINO ACIDS; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; KINETICS; LIGANDS; MODELS, BIOLOGICAL; MUTAGENESIS; NADP; NITRIC OXIDE; OXIDATION-REDUCTION; OXYGEN; OXYGENASES; TIME FACTORS; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034724887     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.17.12581     Document Type: Article

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