Mechanism of extradiol aromatic ring-cleaving dioxygenases

Research output: Contribution to journalReview article

107 Citations (Scopus)

Abstract

The extradiol aromatic ring-cleaving dioxygenases activate molecular oxygen by binding both O2 and the catecholic substrate to a reduced active site metal, generally Fe(II). Progress has been made in understanding the mechanism of this reaction through the combined use of kinetic, computational, biomimetic, structural, and diagnostic chemical approaches. It appears that O2 is activated by accepting an electron transferred from the substrate through the metal, thereby simultaneously activating oxygen and substrate for reaction with each other.

Original languageEnglish (US)
Pages (from-to)644-649
Number of pages6
JournalCurrent Opinion in Structural Biology
Volume18
Issue number6
DOIs
StatePublished - Dec 1 2008

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Dioxygenases
Metals
Oxygen
Biomimetics
Catalytic Domain
Electrons

Cite this

Mechanism of extradiol aromatic ring-cleaving dioxygenases. / Lipscomb, John D.

In: Current Opinion in Structural Biology, Vol. 18, No. 6, 01.12.2008, p. 644-649.

Research output: Contribution to journalReview article

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