Mechanism of extradiol aromatic ring-cleaving dioxygenases

John D. Lipscomb

Research output: Contribution to journalReview articlepeer-review

166 Scopus citations

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 2008

Bibliographical note

Funding Information:
The author would like to thank many students and collaborators who conducted the studies described here in his laboratory. These studies were supported by National Institutes of Health grant GM24689.

Fingerprint

Dive into the research topics of 'Mechanism of extradiol aromatic ring-cleaving dioxygenases'. Together they form a unique fingerprint.

Cite this