Cytochrome P-450 enzymes (EC 1.14. 14.1, nonspecific monooxygenase) catalyze the
oxidations of many chemicals (1). The mass of the substrates ranges from that of ethylene …

This review examines the monooxygenase, peroxidase and peroxygenase properties and
reaction mechanisms of cytochrome P450 (CYP) enzymes in bacterial, archaeal and …

Metalloporphyrins as versatile catalysts for oxidation reactions and oxidative DNA cleavage
Page 1 Chem. Rev. 1992, 92, 1411-1456 1411 Metalloporphyrins as Versatile Catalysts for …

Structural factors that influence functional properties are examined in the case of four heme
enzymes: cytochrome P-450, chloroperoxidase, horseradish peroxidase, and secondary …

This review examines the monooxygenase, peroxidase, and peroxygenase properties of
cytochrome P450 (P450) 1 enzymes and their mechanisms of action in archaeal, bacterial …

The current interest in catalytic oxidative transformations has been stimulated by two major
environmental issues. The first one is the need for replacement of oxidations which use …

The search for practical methods for enantioselective epoxidation of unfunctionalized olefins
continues to present important challenges in the field of catalysis. 1 While recently …

The substrate specificity of chloroperoxidase from Caldaromyces fumago in a number of
halide-independent reactions was investigated and the ability of this enzyme toperform …

The structures of the active sites of horseradish and cytochrome c peroxidase, prototypical
peroxidases with an imidazole heme ligand, suggest that small substrates are generally …

Biological systems have evolved haloperoxidase (HaloPO) enzymes to catalyze the
oxidation of chloride, bromide and iodide by hydrogen peroxide. Recent reviews have been …