Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates

Miquel Costas, Mark P. Mehn, Michael P. Jensen, Lawrence Que

Research output: Contribution to journalReview articlepeer-review

1884 Scopus citations

Abstract

The function of the iron centers of the bacterial catechol dioxygenase enzymes in dioxygen activation was studied. The enzymes were found to convert dihydroxybenzenes into nonaromatic, acyclic compounds, which were then utilized as carbon sources for cell growth. Although these enzymes shared similar substrates, the intradiol- and extradiol-cleving enzymes exhibited near exclusivity in their oxidative cleavage products. The intradiol-cleaving catechol dioxygenases were also found to use an [Fe iii-(His) 2] active site, while extradiol-cleaving catechol dioxygenases contained a [M ii(His) 2(Asp/Glu)] active site.

Original languageEnglish (US)
Pages (from-to)939-986
Number of pages48
JournalChemical Reviews
Volume104
Issue number2
DOIs
StatePublished - Feb 2004

Fingerprint Dive into the research topics of 'Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates'. Together they form a unique fingerprint.

Cite this