Purification and characterization of enzymes involved in desulfurization of dibezothiophene in fossil fuels

DszC and DszA, dibenzothiophene (DBT) and DBT sulfone monooxygenases, respectively, involved in 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.