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An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum.
Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61.
Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases.
Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity.
Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds.
Structural changes common to catalysis in the Tpx peroxiredoxin subfamily.
Engineering of fluorescent reporters into redox domains to monitor electron transfers.
Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.
Escherichia coli Proteins
Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates.
Nitration transforms a sensitive peroxiredoxin 2 into a more active and robust peroxidase.
X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action.