Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase

Elena G. Kovaleva, John D. Lipscomb

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


The reactive oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed by binding the catecholic substrate and O2 in adjacent ligand positions of the active site metal [usually Fe(II)]. This intermediate and the following Fe(II)-alkyl-peroxo intermediate resulting from oxygen attack on the substrate have been previously characterized in a crystal of homoprotocatechuate 2,3-dioxygenase (HPCD). Here a subsequent intermediate in which the O-O bond is broken to yield a gem diol species is structurally characterized. This new intermediate is stabilized in the crystal by using the alternative substrate, 4-sulfonylcatechol, and the Glu323Leu variant of HPCD, which alters the crystal packing.

Original languageEnglish (US)
Pages (from-to)11168-11170
Number of pages3
Issue number43
StatePublished - Oct 28 2008


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