AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low M(r) thioredoxin reductase

European Journal of Biochemistry

Volumn 267, Issue 20, 2000, Pages 6126-6133

  Poole, Leslie B ^a   Michael Reynolds, C ^a   Wood, Zachary A ^b   Andrew Karplus, P ^b   Ellis, Holly R ^a,c   Li Calzi, Marco ^a,d  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b OREGON STATE UNIVERSITY   (United States)

^c TEXAS A AND M UNIVERSITY   (United States)

^d Merck Research Laboratories   (Italy)

Author keywords

AhpC; AhpF; Electron transfer proteins; Flavoproteins; NADH oxidases; Oxidoreductases; Peroxiredoxin; Redox mediators; Redox active disulfide centers; Thioredoxin reductase

Indexed keywords

BACTERIAL PROTEIN; CHIMERIC PROTEIN; ENZYME VARIANT; FLAVOPROTEIN; HYDROPEROXIDE DERIVATIVE; OXIDOREDUCTASE; PEROXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOREDOXIN REDUCTASE;

AMINO TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; REDUCTION; SALMONELLA TYPHIMURIUM; SHORT SURVEY; SPECTROSCOPY;

AMINO ACID SEQUENCE; FLAVOPROTEINS; MODELS, CHEMICAL; MOLECULAR WEIGHT; NADH, NADPH OXIDOREDUCTASES; PEROXIDASES; THIOREDOXIN REDUCTASE (NADPH);

EID: 0033771859     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01704.x     Document Type: Short Survey

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