作者: B D Erickson , F J Mondello
DOI: 10.1128/JB.174.9.2903-2912.1992
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摘要: Abstract The DNA region encoding biphenyl dioxygenase, the first enzyme in biphenyl-polychlorinated degradation pathway of Pseudomonas species strain LB400, was sequenced. Six open reading frames were identified, four which are homologous to components toluene dioxygenase from putida F1 and have been named bphA, bphE, bphF, bphG. From this comparison, found be a multicomponent containing two-subunit iron-sulfur protein, ferredoxin, reductase. Comparison large subunit protein ferredoxin with other dioxygenases identified amino acid sequences similar Rieske proteins for binding [2Fe-2S] cluster. Sequences also reductase component that match consensus sequence FAD or NAD binding. Transcription examined, three transcription initiation sites identified. initiating at site furthest upstream is greatly increased when LB400 cells grown on as sole carbon source.