Kovaleva, Elena G. Lipscomb, John D. Intermediate in the O−O Bond Cleavage Reaction of an Extradiol Dioxygenase<sup>,</sup> The reactive oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed by binding the catecholic substrate and O<sub>2</sub> 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. HPCD;alternative substrate;ligand positions;Fe;oxygen attack;dioxygenase;Glu 323Leu variant;O 2;site metal;catecholic substrate;crystal;gem diol species 2008-10-28
    https://acs.figshare.com/articles/journal_contribution/Intermediate_in_the_O_O_Bond_Cleavage_Reaction_of_an_Extradiol_Dioxygenase_sup_sup_/2904796
10.1021/bi801459q.s001