Oligomeric state and utilization of various substrates by a Bcp‐class peroxiredoxin from Escherichia coli

TL;DRAbstract

Peroxiredoxins (Prx) possess a conserved active site structure centered around the catalytic residue (the “peroxidatic” cysteine) which forms a cysteine sulfenic acid upon reaction with peroxides; this cysteine subsequently forms a disulfide bond with the putative resolving cysteine (either inter‐ or intramolecular) and/or the reductant during reductive recycling. In Escherichia coli , bacterioferritin‐comigratory protein (Bcp) is a peroxiredoxin responsible for catalyzing the reduction of hydrogen peroxide and alkyl hydroperoxides. A second cysteine is located near the active site of E. coli Bcp (conserved in 48% of Bcp homologs) which may or may not serve as a resolving cysteine during catalysis. Analytical ultracentrifugation studies of reduced and oxidized Bcp showed that E. coli Bcp exists as a monomer in solution, eliminating the possibility of intersubunit disulfide bond formation. During thioredoxin‐dependent peroxidase activity studies conducted by stopped flow spectroscopy, a

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