Mutation of conserved tryptophan residues at the dimer interface of Staphylococcus aureus nitric oxide synthase

Archives of Biochemistry and Biophysics

Volumn 506, Issue 2, 2011, Pages 165-172

  Lustig, Daniel Ben ^a,b   Kempt, Cora ^a   Alam, Samiah ^a   Clancy, James ^a   Yee, Janet ^a   Rafferty, Steven Patrick ^a  

^a TRENT UNIVERSITY   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

Bacterial nitric oxide synthase; Hemeprotein; Mutagenesis; Pterin; Quaternary structure

Indexed keywords

ARGININE; DIMER; NITRIC OXIDE SYNTHASE; OXYGENASE; TRYPTOPHAN;

ARTICLE; BINDING AFFINITY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; GENE MUTATION; HYDROGEN BOND; NONHUMAN; OXIDATION; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS; TEMPERATURE;

AMINO ACID SUBSTITUTION; ARGININE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DIMERIZATION; ENZYME ACTIVATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NITRIC OXIDE SYNTHASE; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY; STAPHYLOCOCCUS AUREUS; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS AUREUS;

EID: 79151474975     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2010.11.024     Document Type: Article

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