Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor

Microbial cytochrome c peroxidases (Ccp) have been studied for 75 years, but their physiological roles are unclear. Ccps are located in the periplasms of bacteria and the mitochondrial intermembrane spaces of fungi. In this study, Ccp is demonstrated to be a significant degrader of hydrogen peroxide in anoxic Escherichia coli. Intriguingly, ccp transcription requires both the presence of H₂O₂ and the absence of O₂. Experiments show that Ccp lacks enough activity to shield the cytoplasm from exogenous H₂O₂. However, it receives electrons from the quinone pool, and its flux rate approximates flow to other anaerobic electron acceptors. Indeed, Ccp enabled E. coli to grow on a nonfermentable carbon source when H₂O₂ was supplied. Salmonella behaved similarly. This role rationalizes ccp repression in oxic environments. We speculate that micromolar H₂O₂ is created both biologically and abiotically at natural oxic/anoxic interfaces. The OxyR response appears to exploit this H₂O₂ as a terminal oxidant while simultaneously defending the cell against its toxicity.