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

Elena G. Kovaleva, John D. Lipscomb

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

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
JournalBiochemistry
Volume47
Issue number43
DOIs
StatePublished - Oct 28 2008

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3,4-dihydroxyphenylacetate 2,3-dioxygenase
Dioxygenases
Crystals
Substrates
Gems
Catalytic Domain
Metals
Oxygen
Ligands
extradiol dioxygenase

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Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. / Kovaleva, Elena G.; Lipscomb, John D.

In: Biochemistry, Vol. 47, No. 43, 28.10.2008, p. 11168-11170.

Research output: Contribution to journalArticle

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