Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization.
DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.
Ohshiro
T
T
Department of Biotechnology, Tottori University, Japan.
Izumi
Y
Y
D001673:Biodegradation, Environmental; D003460:Crystallization; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010105:Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D012240:Rhodococcus / Q000201:enzymology*; D013379:Substrate Specificity; D013876:Thiophenes / Q000378:metabolism*
D013876:Thiophenes; D010088:Oxidoreductases; D010105:Oxygenases; C421210:dibenzothiophene sulfone monooxygenase; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases; C090100:dibenzothiophene monooxygenase; C016366:dibenzothiophene