Heme-containing dioxygenases involved in tryptophan oxidation

Elizabeth S. Millett, Igor Efimov, Jaswir Basran, Sandeep Handa, Christopher G. Mowat, Emma Lloyd Raven

Research output: Contribution to journalLiterature reviewpeer-review

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.

Original languageEnglish
Pages (from-to)60-66
Number of pages7
JournalCurrent opinion in chemical biology
Volume16
Issue number1-2
DOIs
Publication statusPublished - Apr 2012

Keywords

  • HUMAN INDOLEAMINE 2,3-DIOXYGENASE
  • REACTION-MECHANISM
  • SUBSTRATE-BINDING
  • CRYSTAL-STRUCTURE
  • MAJOR REDUCTANT
  • CYTOCHROME B(5)
  • MISSING PIECE
  • ACTIVE-SITE
  • ENZYME
  • PEROXIDASE

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