3ecj

Publication Abstract from PubMed

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.

Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase.,Kovaleva EG, Lipscomb JD Biochemistry. 2008 Oct 28;47(43):11168-70. Epub 2008 Oct 1. PMID:18826259^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.