Please use this identifier to cite or link to this item:
Title: Heme-containing dioxygenases involved in tryptophan oxidation.
Authors: Millett, ES
Efimov, I
Basran, J
Handa, S
Mowat, CG
Raven, EL
First Published: Apr-2012
Citation: CURR OPIN CHEM BIOL, 2012, 16 (1-2), pp. 60-66
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.
DOI Link: 10.1016/j.cbpa.2012.01.014
eISSN: 1879-0402
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Chemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.