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• W2065166675 abstract "Phthalate dioxygenase (PDO) is a member of a class of bacterial oxygenases that contain both Rieske [2Fe–2S] and Fe(II) mononuclear centers. Recent crystal structures of several Rieske dioxygenases showed that they exist as α3β3 multimers with subunits arranged head-to-tail in α and β stacked planar rings. The structure of PDO, which consists of only α-subunits, remains to be solved. Although similar to other Rieske dioxygenases in many aspects, PDO was shown to differ in the mechanism of catalysis. Gel filtration and analytical centrifugation experiments, supplemented with mass spectrometric analysis (both ESI-MS and ESI-GEMMA), in this work showed a hexameric arrangement of subunits in the PDO multimer. Our proposed model for the subunit arrangement in PDO postulates two α3 planar rings one on top the other, similar to the α3β3 arrangement in other Rieske dioxygenases. Unlike other Rieske dioxygenases, this arrangement brings two Rieske and two mononuclear centers, all on separate subunits, into proximity, allowing their cooperation for catalysis. Potential reasons necessitating this unusual structural arrangement are discussed." @default.
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• W2065166675 date "2007-10-01" @default.
• W2065166675 modified "2023-10-03" @default.
• W2065166675 title "Similar enzymes, different structures: Phthalate dioxygenase is an α3α3 stacked hexamer, not an α3β3 trimer like “normal” Rieske oxygenases" @default.
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• W2065166675 doi "https://doi.org/10.1016/j.abb.2007.07.001" @default.
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