Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin

Biochemistry

Volumn 50, Issue 41, 2011, Pages 8970-8981

  Reeves, Stacy A ^a   Parsonage, Derek ^a   Nelson, Kimberly J ^a   Poole, Leslie B ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; APPARENT K; BACTERIOFERRITIN; CELLULAR CONDITIONS; CUMENE HYDROPEROXIDE; DEFENSE ENZYME; E. COLI; KINETIC ANALYSIS; MULTIPLE SUBSTRATES; ORGANIC HYDROPEROXIDES; PEROXIDATIC CYSTEINE; PING-PONG MECHANISM; REDOX POTENTIALS; STOPPED FLOW; STRUCTURAL DATA; THIOREDOXINS;

AMINO ACIDS; AROMATIC HYDROCARBONS; CENTRIFUGATION; DIMERS; MONOMERS; PROTEINS; REDOX REACTIONS;

ESCHERICHIA COLI;

BACTERIOFERRITIN COMIGRATORY PROTEIN; CYSTEINE; DIMER; HYDROPEROXIDE; MONOMER; PEROXIDE; PEROXIREDOXIN; THIOREDOXIN 1; THIOREDOXIN 2; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL INTERACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME KINETICS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SPECTROSCOPY; THERMODYNAMICS; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CLONING, MOLECULAR; ESCHERICHIA COLI; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; OXIDATION-REDUCTION; PEROXIDES; PEROXIREDOXINS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS; THIOREDOXINS; ULTRACENTRIFUGATION;

ESCHERICHIA COLI;

EID: 80054771975     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200935d     Document Type: Article

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