Heme-containing Dioxygenases

Igor Efimov*, Jaswir Basran, Sarah J. Thackray, Sandeep Handa, Christopher G. Mowat, Emma Lloyd Raven

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

4 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)33-51
Number of pages19
JournalAdvances in Inorganic Chemistry
Publication statusPublished - 5 Mar 2012


  • Dioxygenases
  • Heme
  • Iron

Fingerprint Dive into the research topics of 'Heme-containing Dioxygenases'. Together they form a unique fingerprint.

Cite this