title: Oxygenases: mechanisms and structural motifs for O(2) activation.
abstract: Recent structural and mechanistic analysis of oxygenase enzymes together with the study of biomimetic model reactions have provided new insights into the catalytic mechanisms of oxygenase-catalysed reactions. High-valent iron-oxo intermediates have been implicated in heme- and pterin-dependent mono-oxygenases. Structural motifs have been identified for binding of non-heme iron(II) (His,His,Glu) and iron(III) (His(2)Tyr(2)) in non-heme-dependent dioxygenases, but additional factors influencing the choice of reaction pathway are emerging from model studies.
authors.affiliation: Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK. mssgv@warwick.ac.uk
authors.forename: T D
authors.initials: TD
authors.lastname: Bugg
mesh_terms: D008956:Models, Chemical; D015394:Molecular Structure; D019159:Nonheme Iron Proteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D010105:Oxygenases / Q000737:chemistry*; D011725:Pyridines / Q000138:chemical synthesis / Q000737:chemistry*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
chemical_list: D019159:Nonheme Iron Proteins; D011725:Pyridines; D010105:Oxygenases; D010100:Oxygen