Journal
BIOCHEMISTRY
Volume 47, Issue 43, Pages 11168-11170Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi801459q
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Funding
- NIGMS NIH HHS [R01 GM024689, R01 GM024689-30, R37 GM024689, GM24689] Funding Source: Medline
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The reactive oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed by binding the catecholic substrate and O-2 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.
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