Myeloperoxidase-derived oxidants rapidly oxidize and disrupt zinc-cysteine/histidine clusters in proteins

Free Radical Biology and Medicine

Volumn 53, Issue 11, 2012, Pages 2072-2080

  Cook, Naomi L ^a   Pattison, David I ^a,b   Davies, Michael J ^a,b  

^a HEART RESEARCH INSTITUTE   (Australia)

^b University of Sydney   (Australia)

Author keywords

Free radicals; Hypochlorous acid; Inflammation; Myeloperoxidase; Protein oxidation; Thiols; Zinc fingers

Indexed keywords

ALCOHOL DEHYDROGENASE; CYSTEINE; HISTIDINE; HYPOBROMOUS ACID; HYPOCHLOROUS ACID; HYPOTHIOCYANOUS ACID; INORGANIC ACID; MONOMER; THIOL; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CHEMICAL REACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME INHIBITION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN TARGETING;

ALCOHOL DEHYDROGENASE; BINDING SITES; BROMATES; CATALYTIC DOMAIN; COORDINATION COMPLEXES; CYSTEINE; HISTIDINE; HYPOCHLOROUS ACID; KINETICS; OXIDANTS; OXIDATION-REDUCTION; PEROXIDASE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; THIOCYANATES;

EID: 84868631078     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.09.033     Document Type: Article

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