Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase

Biochemistry

Volumn 42, Issue 8, 2003, Pages 2475-2484

  Voegtle, Heather L ^a   Sono, Masanori ^a   Adak, Subrata ^b   Pond, Alycen E ^c   Tomita, Takeshi ^e   Perera, Roshan ^a   Goodin, David B ^c   Ikeda Saito, Masao ^d   Stuehr, Dennis J ^b   Dawson, John H ^a,f  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

^b LERNER RESEARCH INSTITUTE   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e TOHOKU UNIVERSITY   (Japan)

^f UNIVERSITY OF SOUTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; COORDINATION REACTIONS; HYDROGEN BONDS; NITROGEN OXIDES; PARAMAGNETIC RESONANCE; SPECTROSCOPIC ANALYSIS;

MUTATION;

ENZYME KINETICS;

CYSTEINE; FERROUS ION; HEME; HEME OXYGENASE; NITRIC OXIDE; PHENYLALANINE; TRYPTOPHAN; TYROSINE;

AEROBIC METABOLISM; ARTICLE; CATALYSIS; CHEMICAL BINDING; CIRCULAR DICHROISM; COMPLEX FORMATION; DEGRADATION KINETICS; DNA ADDUCT; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; GENE MUTATION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; HYDROGEN BOND; INHIBITION KINETICS; LIGATION; METAL BINDING; NERVE CELL; NONHUMAN; OXIDATION KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; RADIATION ABSORPTION; REGULATORY MECHANISM; ULTRAVIOLET RADIATION; WILD TYPE;

CIRCULAR DICHROISM; CYSTEINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HEME; HUMANS; IRON-SULFUR PROTEINS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE TYPE I; OXIDATION-REDUCTION; PHENYLALANINE; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPTOPHAN; TYROSINE;

EID: 0037418534     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0271502     Document Type: Article

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