Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1
作者： Daniel J Ferraro , Eric N Brown , Chi-Li Yu , Rebecca E Parales , David T Gibson
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摘要: Background The initial step involved in oxidative hydroxylation of monoaromatic and polyaromatic compounds by the microorganism Sphingobium yanoikuyae strain B1 (B1), previously known as Sphingomonas Beijerinckia sp. B1, is performed a set multiple terminal Rieske non-heme iron oxygenases. These enzymes share single electron donor system consisting reductase ferredoxin (BPDO-FB1). One oxygenases, biphenyl 2,3-dioxygenase (BPDO-OB1), responsible for B1's ability to dihydroxylate large aromatic compounds, such chrysene benzo[a]pyrene.
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