title: Heme-containing dioxygenases involved in tryptophan oxidation.
abstract: Heme iron is often used in biology for activation of oxygen. The mechanisms of oxygen activation by heme-containing monooxygenases (the cytochrome P450s) are well known, and involve formation of a Compound I species, but information on the heme-containing dioxygenase enzymes involved in tryptophan oxidation lags far behind. In this review, we gather together information emerging recently from structural, mechanistic, spectroscopic, and computational approaches on the heme dioxygenase enzymes involved in tryptophan oxidation. We explore the subtleties that differentiate various heme enzymes from each other, and use this to piece together a developing picture for oxygen activation in this particular class of heme-containing dioxygenases.
authors.affiliation: Department of Chemistry, University of Leicester, Leicester, LE1 7RH, United Kingdom.
authors.forename: Elizabeth S
authors.initials: ES
authors.lastname: Millett
authors.forename: Igor
authors.initials: I
authors.lastname: Efimov
authors.forename: Jaswir
authors.initials: J
authors.lastname: Basran
authors.forename: Sandeep
authors.initials: S
authors.lastname: Handa
authors.forename: Christopher G
authors.initials: CG
authors.lastname: Mowat
authors.forename: Emma Lloyd
authors.initials: EL
authors.lastname: Raven
mesh_terms: D055162:Biocatalysis; D049308:Dioxygenases / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D006418:Heme / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction; D013379:Substrate Specificity; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
chemical_list: D006418:Heme; D014364:Tryptophan; D049308:Dioxygenases