Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: Comparison of selenium and sulfur enzymes

Biochemistry

Volumn 52, Issue 32, 2013, Pages 5472-5481

  Snider, Gregg W ^a   Ruggles, Erik ^a   Khan, Nadeem ^b   Hondal, Robert J ^a  

^a UNIVERSITY OF VERMONT   (United States)

^b DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC ENZYMES; HYDROXYL RADICALS; HYPOBROMOUS ACID; HYPOCHLOROUS ACIDS; IDENTICAL CONDITIONS; OXIDOREDUCTASES; PYRIDINE NUCLEOTIDES; THIOREDOXIN REDUCTASE;

AMINO ACIDS; MAMMALS; MITOCHONDRIA; OXIDANTS; OXIDATION;

ENZYMES;

CYSTINE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; HYPOBROMOUS ACID; HYPOCHLOROUS ACID; HYPOTHIOCYANOUS ACID; NUCLEOPHILE; OXIDIZING AGENT; PEROXYNITRITE; SELENIUM; SELENOCYSTEINE; SULFINIC ACID DERIVATIVE; SULFUR; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; ENZYME ACTIVITY; ENZYME METABOLISM; MITOCHONDRION; NONHUMAN; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL;

ANIMALS; CATALYSIS; DROSOPHILA MELANOGASTER; HYDROGEN PEROXIDE; KINETICS; MICE; OXIDATION-REDUCTION; SELENOCYSTEINE; SULFUR; THIOCYANATES; THIOREDOXIN-DISULFIDE REDUCTASE;

EID: 84881657606     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400462j     Document Type: Article

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