The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway-the O 2-dependent oxidation of l-tryptophan to N-formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a number of dioxygenases, contributions from computational chemistry, and emerging mechanistic data from site-directed mutagenesis. This review summarizes these recent contributions.
|Number of pages||19|
|Journal||Advances in Inorganic Chemistry|
|Publication status||Published - 5 Mar 2012|