Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: Role of a thioredoxin domain in disulfide bond formation

Biochemistry

Volumn 42, Issue 15, 2003, Pages 4560-4568

  Raje, Sonali ^a   Thorpe, Colin ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BOND FORMATION;

CATALYST ACTIVITY; CHEMICAL BONDS; ENZYMES; HYDROGEN PEROXIDE; OXIDATION; PHOTOCHEMICAL REACTIONS; REDUCTION;

BIOCHEMISTRY;

DITHIOTHREITOL; ESSENTIAL FOR RESPIRATION AND VIABILITY IN YEAST PROTEIN; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; FUNGAL PROTEIN; HYDROGEN PEROXIDE; OXYGEN; PEPTIDE FRAGMENT; PROTEIN DISULFIDE ISOMERASE; RESERPINE; RIBONUCLEASE; THIOL DERIVATIVE; THIOL OXIDASE; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; DISULFIDE BOND; ELECTRON TRANSPORT; ENZYME ACTIVITY; MOLECULAR WEIGHT; OXIDATION REDUCTION REACTION; PHOTOOXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN GLYCOSYLATION; PROTEIN MOTIF;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CHICKENS; CYSTINE; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY; THIOREDOXIN;

AVES;

EID: 0037461350     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030003z     Document Type: Article

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