Site-specific hypochlorous acid-induced oxidation of recombinant human myoglobin affects specific amino acid residues and the rate of cytochrome b5-mediated heme reduction

Free Radical Biology and Medicine

Volumn 48, Issue 1, 2010, Pages 35-46

  Szuchman Sapir, Andrea J ^a   Pattison, David I ^b   Davies, Michael J ^b,c   Witting, Paul K ^a,c  

^a Department of Microbiology and Infectious Diseases   (Australia)

^b HEART RESEARCH INSTITUTE   (Australia)

^c University of Sydney   (Australia)

Author keywords

Amino acid modification; Free radicals; Heme reduction; Hypochlorous acid; MetMb reductase; Myoglobin; Protein oxidation

Indexed keywords

ALANINE; CHLORAMINE DERIVATIVE; CYSTEINE; CYTOCHROME B5; FERRIC ION; HEME; HYPOCHLOROUS ACID; METHIONINE; MYOGLOBIN; RECOMBINANT PROTEIN; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; TRYPTOPHAN; TYROSINE;

ARTICLE; CHLORINATION; CONTROLLED STUDY; HUMAN; OXIDATION KINETICS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MODIFICATION; WILD TYPE;

AMINO ACIDS; CYTOCHROMES B5; HEME; HUMANS; HYPOCHLOROUS ACID; IRON; MYOGLOBIN; OXIDATION-REDUCTION; RECOMBINANT PROTEINS;

EID: 74149089247     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.09.023     Document Type: Article

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