Utilization of organosulphur compounds by axenic and mixed cultures of Rhodococcus rhodochrous IGTS8

Kayser, Kevin J.; Bielaga-Jones, Barbara A.; Jackowski, Kathy; Odusan, Opeoluwa; Kilbane, John J.

doi:10.1099/00221287-139-12-3123

Cited by 182 publications

(105 citation statements)

References 9 publications

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“…The gram-positive bacterium Rhodococcus sp. strain IGTS8 desulfurizes DBT by a biochemical pathway that is similar, but not identical, to the 4S pathway, with 2HBP being one end product of the reaction (3,8,15,19,20).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8

et al. 1994

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Rhodococcus sp. strain IGTS8 possesses an enzymatic pathway that can remove covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. The DNA sequence of a 4.0-kb BstBI-BsiWI fragment that carries the genes for this pathway was determined. Frameshift and deletion mutations established that three open reading frames were required for DBT desulfurization, and the genes were designated soxABC (for sulfur oxidation). Each sox gene was subcloned independently and expressed in Escherichia coli MZ1 under control of the inducible lambda pL promoter with a lambda cII ribosomal binding site. SoxC is an approximately 45-kDa protein that oxidizes DBT to DBT-5,5'-dioxide. SoxA is an approximately 50-kDa protein responsible for metabolizing DBT-5,5'-dioxide to an unidentified intermediate. SoxB is an approximately 40-kDa protein that, together with the SoxA protein, completes the desulfurization of DBT-5,5'-dioxide to 2-hydroxybiphenyl. Protein sequence comparisons revealed that the predicted SoxC protein is similar to members of the acyl coenzyme A dehydrogenase family but that the SoxA and SoxB proteins have no significant identities to other known proteins. The sox genes are plasmidborne and appear to be expressed as an operon in Rhodococcus sp. strain IGTS8 and in E. coli.

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Section: Discussionmentioning

confidence: 99%

Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8

et al. 1994

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“…Several species of bacteria that can utilize indole, pyridine, quinoline, and carbazole and its alkyl derivatives have been isolated and characterized, including Alcaligenes, Bacillus, Beijerinckia, Burkholderia, Comamonas, Mycobacterium, Pseudomonas, Serratia, and Xanthomonas (6,66,190,222,299,311,457,480,511,563,619). Bacteria exhibit some general similarities in the pathways for the transformation of aromatic compounds.…”

Section: Microbial Denitrogenationmentioning

confidence: 99%

“…strain IGTS8 are associated with the external hydrophobic membrane surfaces (148,311,459), it has been hypothesized that the enzymes should be active in nonaqueous media. The maximum oil-water ratio for desulfurization was found to be 1.25 ml/g.…”

Section: Microbial Desulfurizationmentioning

confidence: 99%

Recent Advances in Petroleum Microbiology

Hamme¹,

Singh

Ward

2003

Microbiol Mol Biol Rev

1,201

640

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Recent advances in molecular biology have extended our understanding of the metabolic processes related to microbial transformation of petroleum hydrocarbons. The physiological responses of microorganisms to the presence of hydrocarbons, including cell surface alterations and adaptive mechanisms for uptake and efflux of these substrates, have been characterized. New molecular techniques have enhanced our ability to investigate the dynamics of microbial communities in petroleum-impacted ecosystems. By establishing conditions which maximize rates and extents of microbial growth, hydrocarbon access, and transformation, highly accelerated and bioreactor-based petroleum waste degradation processes have been implemented. Biofilters capable of removing and biodegrading volatile petroleum contaminants in air streams with short substrate-microbe contact times (<60 s) are being used effectively. Microbes are being injected into partially spent petroleum reservoirs to enhance oil recovery. However, these microbial processes have not exhibited consistent and effective performance, primarily because of our inability to control conditions in the subsurface environment. Microbes may be exploited to break stable oilfield emulsions to produce pipeline quality oil. There is interest in replacing physical oil desulfurization processes with biodesulfurization methods through promotion of selective sulfur removal without degradation of associated carbon moieties. However, since microbes require an environment containing some water, a two-phase oil-water system must be established to optimize contact between the microbes and the hydrocarbon, and such an emulsion is not easily created with viscous crude oil. This challenge may be circumvented by application of the technology to more refined gasoline and diesel substrates, where aqueous-hydrocarbon emulsions are more easily generated. Molecular approaches are being used to broaden the substrate specificity and increase the rates and extents of desulfurization. Bacterial processes are being commercialized for removal of H2S and sulfoxides from petrochemical waste streams. Microbes also have potential for use in removal of nitrogen from crude oil leading to reduced nitric oxide emissions provided that technical problems similar to those experienced in biodesulfurization can be solved. Enzymes are being exploited to produce added-value products from petroleum substrates, and bacterial biosensors are being used to analyze petroleum-contaminated environments

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“…The degradation pathways and degradative genes of polycyclic aromatic hydrocarbons and biphenyl derivatives have been well studied (5,14,22,26,30,34,35,51). On the other hand, the catabolic pathways of heterocyclic aromatic compounds such as dibenzothiophene are established (29,40), but there is little information on the degradative genes of these compounds (11).…”

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confidence: 99%

Cloning of genes involved in carbazole degradation of Pseudomonas sp. strain CA10: nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase

et al. 1997

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The DNA fragment encoding meta-cleavage enzymes and the meta-cleavage compound hydrolase, involved in carbazole degradation, was cloned from the carbazole-utilizing bacterium Pseudomonas sp. strain CA10. DNA sequence analysis of this 2.6-kb SmaI-SphI fragment revealed that there were three open reading frames (ORF1, ORF2, and ORF3, in this gene order). ORF1 and ORF2 were indispensable for meta-cleavage activity for 2-aminobiphenyl-2,3-diol and its easily available analog, 2,3-dihydroxybiphenyl, and were designated carBa and carBb, respectively. The alignment of CarBb with other meta-cleavage enzymes indicated that CarBb may have a non-heme iron cofactor coordinating site. On the basis of the phylogenetic tree, CarBb was classified as a member of the protocatechuate 4,5-dioxygenase family. This unique extradiol dioxygenase, CarB, had significantly higher affinity and about 20-times-higher meta-cleavage activity for 2,3-dihydroxybiphenyl than for catechol derivatives. The putative polypeptide encoded by ORF3 was homologous with meta-cleavage compound hydrolases in other bacteria, and ORF3 was designated carC. The hydrolase activity of CarC for 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, the meta-cleavage compound of 2,3-dihydroxybiphenyl, was 40 times higher than that for 2-hydroxy-6-oxohepta-2,4-dienoic acid, the meta-cleavage compound of 3-methylcatechol. Alignment analysis and the phylogenetic tree indicate that CarC has greatest homologies with hydrolases involved in the monoaromatic compound degradation pathway. These results suggest the possibility that CarC is a novel type of hydrolase.

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Utilization of organosulphur compounds by axenic and mixed cultures of Rhodococcus rhodochrous IGTS8

Cited by 182 publications

References 9 publications

Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8

Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8

Recent Advances in Petroleum Microbiology

Cloning of genes involved in carbazole degradation of Pseudomonas sp. strain CA10: nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase

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