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Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase.
Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis.
An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum.
Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases.
Structural changes common to catalysis in the Tpx peroxiredoxin subfamily.
Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.
A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope.
Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes.
Sequence Homology, Amino Acid
An Atlas of Peroxiredoxins Created Using an Active Site Profile-Based Approach to Functionally Relevant Clustering of Proteins.