Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function

Biochemistry

Volumn 44, Issue 30, 2005, Pages 10339-10348

  Brokx, Stephen J ^a   Rothery, Richard A ^a   Zhang, Guijin ^a   Ng, Derek P ^a   Weiner, Joel H ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOCHEMISTRY; BIOLOGICAL MEMBRANES; ELECTRON RESONANCE; ENZYMES;

SOLUBLE CATALYTIC SUBUNIT; SULFITE OXIDASE HOMOLOGUE; TAT TRANSLOCATION SYSTEM; TWIN ARGININE LEADER SEQUENCE;

ESCHERICHIA COLI;

ARGININE; CYSTEINE; CYTOCHROME B; MOLYBDENUM; SULFITE OXIDASE;

ARTICLE; BACTERIAL GENE; BACTERIAL TRANSLOCATION; CYTOPLASM; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ESCHERICHIA COLI; GENE ISOLATION; GENE MUTATION; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; YEDYZ GENE;

BINDING SITES; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; CYSTEINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI PROTEINS; HISTIDINE; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON SULFUR GROUP DONORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SERINE; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; TUNGSTEN;

ESCHERICHIA COLI;

EID: 23044485986     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050621a     Document Type: Article

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