Disease relevance of dibenzothiophene

• The desulfurization of dibenzothiophene in Rhodococcus erythropolis is catalyzed by two monooxygenases, DszA and DszC, and a desulfinase, DszB [1].
• Mycobacterium goodii X7B, which had been primarily isolated as a bacterial strain capable of desulfurizing dibenzothiophene to produce 2-hydroxybiphenyl via the 4S pathway, was also found to desulfurize benzothiophene [2].
• Plasmid-mediated degradation of dibenzothiophene by Pseudomonas species [3].
• While the ssu genes encode proteins resembling Ssu proteins from Escherichia coli or Bacillus subtilis, the seu gene products exhibited similarity to the dibenzothiophene-degrading Dsz monooxygenases of Rhodococcus strain IGTS8 [4].
• Desulfurization of dibenzothiophene by Corynebacterium sp. strain SY1 [5].

High impact information on dibenzothiophene

• Equilibrium studies on the series of [CpRu(CO)(2)(eta(1)(S)-DBTh)](+) compounds, where DBTh = DBT, 4-MeDBT, 4,6-Me(2)DBT, and 2,8-Me(2)DBT, show that the relative binding strengths of the dibenzothiophene ligands increase in the order 4,6-Me(2)DBT (1) < 4-MeDBT (20.2(1)) < DBT (62.7(6)) < 2,8-Me(2)DBT (223(3)) [6].
• X-ray studies of 1 and its 4-methyldibenzothiophene and dibenzothiophene analogues, [CpRu(CO)(2)(eta(1)(S)-4-MeDBT)]BF(4) (2) and [CpRu(CO)(2)(eta(1)(S)-DBT)]BF(4) (3), show that the Ru-S bond distances increase in the order, 3 < 2 < 1 [6].
• The sonochemically prepared catalysts were characterized by elemental analysis, XPS, SEM, TEM, and XEDS, and hydrodesulfurization (HDS) activity evaluated for thiophene and dibenzothiophene substrates [7].
• The dibenzothiophene 32{38} sensitized HeLa cells to ionizing radiation in vitro, with dose modification factors of 2.5 at 10% survival being observed at 0.5 microM [8].
• The resultant strain, Rhodococcus erythropolis XPDN, could simultaneously transform the model pollutants dibenzothiophene, carbazole, and dibenzofuran to nontoxic metabolites and may have an application potential for bioremediation [9].

Chemical compound and disease context of dibenzothiophene

• The recombinant Rhodococcus erythropolis SN8 was capable of efficiently degrading dibenzothiophene and carbazole simultaneously [10].
• Purification, characterization, and overexpression of flavin reductase involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-1 [11].
• The oxidation of dibenzothiophene to dibenzothiophene sulfone has been linked to the enzyme encoded by the sox/dszC gene from Rhodococcus sp. strain IGTS8 (S. A. Denome, C. Oldfield, L. J. Nash, and K. D. Young, J. Bacteriol. 176:6707-6717, 1994; C. S. Piddington, B. R. Kovacevich, and J. Rambosek, Appl. Environ. Microbiol. 61:468-475, 1995) [12].
• Four known dibenzothiophene-desulfurizing strains, including Rhodococcus sp. strain IGTS8, were all unable to cleave the C-S bond in PFPS but could oxidize PFPS to the sulfone via the sulfoxide [13].
• The methods developed to extract and detect these three disulfides were then used for the analysis of a culture of Pseudomonas sp. strain BT1d grown on dibenzothiophene as its sole carbon and energy source [14].

Biological context of dibenzothiophene

• Sequence and molecular characterization of a DNA region encoding the dibenzothiophene desulfurization operon of Rhodococcus sp. strain IGTS8 [15].
• The dsz gene cluster of Rhodococcus erythropolis IGTS8 comprises three genes, dszA, dszB, and dszC, whose products are involved in the conversion of dibenzothiophene (DBT) to 2-hydroxybiphenyl and sulfite [16].
• Frameshift and deletion mutations established that three open reading frames were required for DBT desulfurization, and the genes were designated soxABC (for sulfur oxidation) [17].
• [figure: see text] Direct synthetic access to 2-hydroxy-alpha-mannopyranosides from glucal donors is accomplished via a one-pot stereoselective oxidative glycosylation reaction, employing the reagent combination of dibenzothiophene bis(triflate) and dibenzothiophene-5-oxide [18].
• The deduced amino acid sequence of IBAH exhibited the greatest similarity to the Sox/DszC protein from Rhodococcus sp. strain IGT38, a flavoprotein involved in the oxidation of dibenzothiophene to the corresponding sulfone [19].

Anatomical context of dibenzothiophene

• The mutagenic activity of some of these compounds, including dibenzothiophene, benzo[b]naphtho[1,2-d]thiophene, benzo[b]naphtho[2,1-d]thiophene and benzo[b]naphtho[2,3-d]thiophene have been determined using the Salmonella/microsome mutagenicity test [20].
• Methods and Results: In the present study, dibenzothiophene (DBT) desulfurizing activity, composition of fatty acids of cell membranes, DBT sulfone monoxygenase gene (bdsA) and the selection pressure applied during the growth and enrichment of the bacterial strains M. phlei SM120-1 and M. phlei GTIS10 were compared in our laboratory [21].
• In this study, biodesulfurization (BDS) was carried out using immobilized Rhodococcus erythropolis KA2-5-1 in n-tetradecane containing dibenzothiophene (DBT) as a model oil (n-tetradecane/immobilized cell biphasic system) [22].

Associations of dibenzothiophene with other chemical compounds

• SN8 could also degrade various alkylated derivatives of carbazole and dibenzothiophene in FS4800 crude oil by just a one-step bioprocess [10].
• Radical cation of dibenzothiophene fully annelated with bicyclo[2.2.2]octene units: X-ray crystal structure and electronic properties [23].
• The primary etiology of defects induced by dibenzothiophene or phenanthrene appears to be direct effects on cardiac conduction, which have secondary consequences for late stages of cardiac morphogenesis, kidney development, neural tube structure, and formation of the craniofacial skeleton [24].
• The dibenzothiophene (DBT) desulfurizing operon, dsz, was introduced into various benzothiophene (BT)-desulfurizing bacteria using a Rhodococcus-E. coli shuttle vector [25].
• The total sulfur level of dibenzothiophene in tetradecane, was reduced by 99%, from 200 to 2ppm within 24h at 40 degrees C. After 72h treatment, 59% of the total sulfur content in Liaoning crude oil was removed, from 3600 to 1478ppm [26].

Gene context of dibenzothiophene

• Biodesulfurization of dibenzothiophene in Escherichia coli is enhanced by expression of a Vibrio harveyi oxidoreductase gene [27].
• Exposure to the three-ring PAHs dibenzothiophene and phenanthrene alone was sufficient to induce the characteristic suite of defects, as was genetic ablation of cardiac function using a cardiac troponin T antisense morpholino oligonucleotide [24].
• P450 catalysed S-oxidation of dibenzothiophene by Cunninghamella elegans [28].
• The gene encoding NAD(P)H-flavin oxidoreductase (flavin reductase), which couples efficiently with dibenzothiophene (DBT)-desulfurizing monooxygenases of Rhodococci, was cloned from a DBT-non-desulfurizing bacterium Paenibacillus polymyxa A-1 in Escherichia coli, and designated as flv [29].
• The gene encoding the NAD(P)H-flavin oxidoreductase (flavin reductase) which couples with the thermophilic dibenzothiophene (DBT)-desulfurizing monooxygenases of Paenibacillus sp. A11-2 was cloned in Escherichia coli and designated tdsD [30].

Analytical, diagnostic and therapeutic context of dibenzothiophene

• The cloned sulfur oxidation (desulfurization) genes (sox) for dibenzothiophene (DBT) from the prototype Rhodococcus sp. strain IGTS8 were used in Southern hybridization and PCR experiments to establish the DNA relatedness in six new rhodococcal isolates which are capable of utilizing DBT as a sole sulfur source for growth [31].
• New dibenzothiophene 2 fully annelated with bicyclo[2.2.2]octene units was synthesized and oxidized to stable radical cation salt 2(*+)SbCl(6)(-), whose structure was determined by X-ray crystallography [23].
• Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization [32].
• This result was consistent with results of Western-blot analysis using antisera specific for DszA, DszB and DszC, the enzymes involved in the desulfurization of dibenzothiophene [33].
• Monooxygenation metabolites of pyrene, dibenzothiophene, and 7-methylbenz[alpha]anthracene were detected in whole cell biotransformations, with E. coli expressing pipA or cyp150 when analyzed by gas chromatography/mass spectrometry [34].

References