Structure, mechanism and physiological roles of bacterial cytochrome c peroxidases.

作者: John M. Atack , David J. Kelly

DOI: 10.1016/S0065-2911(06)52002-8

关键词:

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

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