Peroxidase: a term of many meanings.
Peroxidase research has been instrumental in defining the principles of chemical catalysis. By now, enzymes termed peroxidases represent a heterogeneous group of distinct enzyme families that operate by different catalytic principles and fulfill diverse biological functions, detoxifying H2O2 being just one of many aspects. H2O2 -dependent synthesis of secondary metabolites is the domain of heme peroxidases and related enzymes operating by transition metal catalysis, that often is mediated by free radical formation. Instead, the coenzyme-free glutathione peroxidases and peroxiredoxins only catalyze two-electron transitions and, thus, can reliably remove hydroperoxides without causing radical-mediated collateral damage. However, their ability to use hydroperoxides for the formation of specific disulfide bonds with and within particular proteins broadens their spectrum of biological activities to differentiation phenomena, redox regulation of metabolic processes, redox sensing, and signalling. The present Forum Editorial tries to guide the reader through the 190 years of equally bewildering and fascinating research on peroxidases up to the topical frontiers of the field that are addressed in this issue.
Flohé
Leopold
L
Ursini
Fulvio
F
D000818:Animals; D000975:Antioxidants / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism*; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D054464:Peroxiredoxins / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism
D000975:Antioxidants; D017382:Reactive Oxygen Species; D013879:Thioredoxins; D006861:Hydrogen Peroxide; D010544:Peroxidases; D054464:Peroxiredoxins; D005979:Glutathione Peroxidase