Biochemical characterization of the biodesulfurization of dibenzothiophene by Rhodococcus sp. strain IGTS8
- Energy BioSystems Corp., The Woodlands, TX (United States)
The Gram-positive organism Rhodococcus sp. IGTS8 catalyzes the removal of sulfur from organic components in fossil fuels (middle distillate). One of the major classes of sulfur containing molecules in middle distillate are the alkylated dibenzothiophenes. Unsubstituted dibenzothiophene (DBT) is the usual model compound for studies on this class of molecules. A pathway has been discovered that utilizes a multienzyme system of which the first enzyme, DBT monooxygenase (encoded by dszC), converts DBT to DBT-5,5-dioxide in two discrete steps. The third step involves the conversion of DBT- 5,5-dioxide to 2-(2-hydroxyphenyl)benzenesulfinic acid (PPS) catalyzed by DBT-5,5-dioxide monooxygenase (encoded by dszA). The final enzyme, DSZB, catalyzes the removal of -SO{sub 2} from PPS to form HBP and sulfite. The first two enzymes in the pathway require molecular oxygen, NADH, FMN and an NADH-FMN oxidoreductase while the third enzyme requires no cofactors. The results of purification and kinetic and physical characterization of each enzyme are reported.
- OSTI ID:
- 538946
- Report Number(s):
- CONF-960807--
- Country of Publication:
- United States
- Language:
- English
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