Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase.
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Kovaleva EG, Lipscomb JD
Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase.
Biochemistry. 2008 Oct 28;47(43):11168-70. doi: 10.1021/bi801459q. Epub 2008 Oct 1.
- PubMed ID
- 18826259 [ View in PubMed]
- 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)-alkylperoxo 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.