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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization. Ohshiro, T., Izumi, Y. Bioseparation (2000) [Pubmed]
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