Characterization of Active Recombinant His-tagged Oxygenase Component of Comamonas testosteroni B-356 Biphenyl Dioxygenase

Biphenyl (BPH) dioxygenase oxidizes BPH to 2,3-dihydro-2,3-dihydroxybiphenyl in Comamonas testosteroni B-356. The enzyme comprises a two-subunit iron-sulfur protein (ISP ), a ferredoxin FER , and a ferredoxin reductase RED . RED and FER transfer electrons from NADH to an Fe-S active center of ISP wh...

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Veröffentlicht in:	The Journal of biological chemistry 1996-04, Vol.271 (14), p.8152-8156
Hauptverfasser:	Hurtubise, Y, Barriault, D, Sylvestre, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Base Sequence Comamonas testosteroni DNA Primers - chemistry Gram-Negative Aerobic Bacteria - chemistry Histidine - chemistry Kinetics Molecular Sequence Data Multienzyme Complexes - chemistry Oxygenases - chemistry Recombinant Proteins Spectrum Analysis Structure-Activity Relationship
Online-Zugang:	Volltext
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