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)

Abstract

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
Volume64
DOIs
Publication statusPublished - 5 Mar 2012

Keywords

  • Dioxygenases
  • Heme
  • Iron

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