Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes

Spencer C. Peck, Wilfred A. van der Donk

Research output: Contribution to journalReview article

Abstract

This review discusses the current mechanistic understanding of a group of mononuclear non-heme iron-dependent enzymes that catalyze four-electron oxidation of their organic substrates without the use of any cofactors or cosubstrates. One set of enzymes acts on α-ketoacid-containing substrates, coupling decarboxylation to oxygen activation. This group includes 4-hydroxyphenylpyruvate dioxygenase, 4-hydroxymandelate synthase, and CloR involved in clorobiocin biosynthesis. A second set of enzymes acts on substrates containing a thiol group that coordinates to the iron. This group is comprised of isopenicillin N synthase, thiol dioxygenases, and enzymes involved in the biosynthesis of ergothioneine and ovothiol. The final group of enzymes includes HEPD and MPnS that both carry out the oxidative cleavage of the carbon–carbon bond of 2-hydroxyethylphosphonate but generate different products. Commonalities amongst many of these enzymes are discussed and include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species.

Original languageEnglish (US)
Pages (from-to)381-394
Number of pages14
JournalJournal of Biological Inorganic Chemistry
Volume22
Issue number2-3
DOIs
StatePublished - Apr 1 2017

Fingerprint

Iron
Electrons
Oxidation
Enzymes
Biosynthesis
Substrates
Sulfhydryl Compounds
4-Hydroxyphenylpyruvate Dioxygenase
Ergothioneine
Dioxygenases
Decarboxylation
Chemical activation
Oxygen

Keywords

  • Ferryl
  • Iron oxo
  • Non-heme iron
  • Oxidase
  • Oxygenase
  • Superoxo

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Go it alone : four-electron oxidations by mononuclear non-heme iron enzymes. / Peck, Spencer C.; van der Donk, Wilfred A.

In: Journal of Biological Inorganic Chemistry, Vol. 22, No. 2-3, 01.04.2017, p. 381-394.

Research output: Contribution to journalReview article

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