Post-translational self-hydroxylation: A probe for oxygen activation mechanisms in non-heme iron enzymes

Erik R. Farquhar, Kevin D. Koehntop, Joseph P. Emerson, Lawrence Que

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations


Recent years have seen considerable evolution in our understanding of the mechanisms of oxygen activation by non-heme iron enzymes, with high-valent iron-oxo intermediates coming to the forefront as formidably potent oxidants. In the absence of substrate, the generation of vividly colored chromophores deriving from the self-hydroxylation of a nearby aromatic amino acid for a number of these enzymes has afforded an opportunity to discern the conditions under which O2 activation occurs to generate a high-valent iron intermediate, and has provided a basis for a rigorous mechanistic examination of the oxygenation process. Here, we summarize the current evidence for self-hydroxylation processes in both mononuclear non-heme iron enzymes and in mutant forms of ribonucleotide reductase, and place it within the context of our developing understanding of the oxidative transformations accomplished by non-heme iron centers.

Original languageEnglish (US)
Pages (from-to)230-239
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Dec 9 2005


  • Non-heme iron
  • Oxygen activation
  • Post-translational modification
  • Ribonucleotide reductase
  • Self-hydroxylation
  • α-Ketoglutarate dependent enzymes


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