title: Molecular mechanisms of biocatalytic desulfurization of fossil fuels.
abstract: The development of biocatalytic desulfurization of petroleum fractions may allow its use in place of conventional hydrodesulfurization (HDS). Dibenzothiophene (DBT) is representative of a broad range of sulfur heterocycles found in petroleum that are recalcitrant to desulfurization via HDS. Rhodococcus sp. strain IGTS8 has the ability to convert DBT to 2-hydroxybiphenyl (HBP) with the release of inorganic sulfur. The conversion of DBT to HBP is catalyzed by a multienzyme pathway consisting of two monooxygenases and a desulfinase. The final reaction catalyzed by the desulfinase appears to be the rate limiting step in the pathway. Each of the enzymes has been purified to homogeneity and their kinetic and physical properties studied. Neither monooxygenase has a tightly bound cofactor and each requires an NADH-FMN oxidoreductase for activity. An NADH-FMN oxidoreductase has been purified from Rhodococcus and is a protein of approximately 25,000 molecular weight with no apparent sequence homology to any other protein in the databases. We describe a unique sulfur acquisition system that Rhodococcus uses to obtain sulfur from very stable heterocyclic molecules.
authors.affiliation: Energy BioSystems Corporation, Woodlands, TX 77381, USA. kagray@main.com
authors.forename: K A
authors.initials: KA
authors.lastname: Gray
authors.forename: O S
authors.initials: OS
authors.lastname: Pogrebinsky
authors.forename: G T
authors.initials: GT
authors.lastname: Mrachko
authors.forename: L
authors.initials: L
authors.lastname: Xi
authors.forename: D J
authors.initials: DJ
authors.lastname: Monticello
authors.forename: C H
authors.initials: CH
authors.lastname: Squires
mesh_terms: D001673:Biodegradation, Environmental; D001713:Biphenyl Compounds / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry* / Q000302:isolation & purification; D038181:FMN Reductase; D005579:Fossil Fuels / Q000032:analysis*; D007700:Kinetics; D009097:Multienzyme Complexes / Q000737:chemistry; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D010578:Petroleum / Q000032:analysis; D012240:Rhodococcus / Q000201:enzymology*; D013455:Sulfur / Q000032:analysis*; D013876:Thiophenes / Q000737:chemistry*; D001426:Bacterial Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors
chemical_list: D001713:Biphenyl Compounds; D003574:Cytochrome c Group; D038181:FMN Reductase; D005579:Fossil Fuels; D009097:Multienzyme Complexes; D009247:NADH, NADPH Oxidoreductases; D010088:Oxidoreductases; D010578:Petroleum; D013455:Sulfur; D013876:Thiophenes; C004369:2-phenylphenol; C113832:2-(2-hydroxybiphenyl)-benzenesulfinate desulfinase; D001426:Bacterial Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors; C113628:dibenzothiophene dioxide monooxygenase; C064500:flavocytochrome c sulfide dehydrogenase; C016366:dibenzothiophene