Structure, mechanism and physiological roles of bacterial cytochrome c peroxidases

Abstract

Cytochrome-c peroxidases (CCPs) are a widespread family of enzymes that catalyse the conversion of hydrogen peroxide (H2O2) to water using haem co-factors. CCPs are found in both eukaryotes and prokaryotes, but the enzymes in each group use a distinct mechanism for catalysis. Eukaryotic CCPs contain a single b-type haem co-factor. Conventional bacterial CCPs (bCCPs) are periplasmic enzymes that contain two covalently bound c-type haems. However, we have identified a sub-group of bCCPs by phylogenetic analysis that contains three haem-binding motifs. Although the structure and mechanism of several bacterial di-haem CCPs has been studied in detail and is well understood, the physiological role of these enzymes is often much less clear, especially in comparison to other peroxidatic enzymes such as catalase and alkyl-hydroperoxide reductase. In this review, the structure, mechanism and possible roles of bCCPs are examined in the context of their periplasmic location, the regulation of their synthesis by oxygen and their particular function in pathogens.