Spectral and kinetic studies of the oxidation of monosubstituted phenols and anilines by recombinant Synechocystis catalase-peroxidase compound I

Research was conducted to determine a high-level expression in Escherichia coli of a fully active recombinant form of a catalase-peroxidase (KatG) from the cyanobacterium Synechocystic PCC 6803. Its identity with the wild-type protein was revealed by physical and kinetic characterization. The spectral characteristics of KatG compounds I and II and the rates of reaction of 11 aromatic donor molecules with Synechocystis KatG compound I, determined by sequential-mixing stopped-flow spectroscopy, are described.