Operon Structure and Functional Analysis of the Genes Encoding Thermophilic Desulfurizing Enzymes of Paenibacillus sp. A11-2

Ishii, Yoshitaka; Konishi, Jin; Okada, Hideki; Hirasawa, Kazuaki; Onaka, Toshimitu; Suzuki, Masanori

doi:10.1006/bbrc.2000.2370

Cited by 94 publications

(44 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, SfnC also showed identity with two bacterial FMNH 2 -dependent monooxygenases: TdsC (47 %) from Paenibacillus sp. strain A11-2 (Ishii et al, 2000) and DszC (43 %) from Rhodococcus sp. strain IGTS8 (Demone et al, 1994), both of which catalyse stepwise monooxygenation of dibenzothiophene to dibenzothiophene sulfone.…”

Section: Resultsmentioning

confidence: 99%

A CysB-regulated and σ54-dependent regulator, SfnR, is essential for dimethyl sulfone metabolism of Pseudomonas putida strain DS1

et al. 2003

View full text Add to dashboard Cite

Pseudomonas putida strain DS1 utilizes dimethyl sulfide (DMS) as a sulfur source, and desulfurizes it via dimethyl sulfoxide (DMSO), dimethyl sulfone (DMSO 2 ) and methanesulfonate (MSA). Its Tn5 mutant, Dfi74J, no longer utilized DMS, DMSO and DMSO 2 , but could oxidize DMS to DMSO 2 , suggesting that the conversion of DMSO 2 to MSA was interrupted in the mutant. Sequencing of the Tn5 flanking region of Dfi74J demonstrated that a gene, sfnR (designated for dimethyl sulfone utilization), encoding a transcriptional regulator containing an ATP-dependent s 54 -association domain and a DNA-binding domain, was disrupted. sfnR is part of an operon with two other genes, sfnE and sfnC, located immediately upstream of sfnR and in the same orientation. The genes encode NADH-dependent FMN reductase (SfnE) and FMNH 2 -dependent monooxygenase (SfnC). Complementation of Dfi74J with an sfnR-expressing plasmid led to restoration of its growth on DMS, DMSO and DMSO 2 . An rpoN-defective mutant of strain DS1, which lacks the s 54 factor, grew on MSA, but not on DMS, DMSO and DMSO 2 , indicating that SfnR controls expression of gene(s) involved in DMSO 2 metabolism by interaction with s 54 -RNA polymerase. Northern hybridization and a reporter gene assay with an sfn-lacZ transcriptional fusion elucidated that expression of the sfnECR operon was induced under sulfate limitation and was dependent on a LysR-type transcriptional regulator, CysB. This is believed to be the first report that a s 54 -dependent transcriptional regulator induced under sulfate limitation is involved in sulfur assimilation.

show abstract

Section: Resultsmentioning

confidence: 99%

A CysB-regulated and σ54-dependent regulator, SfnR, is essential for dimethyl sulfone metabolism of Pseudomonas putida strain DS1

et al. 2003

View full text Add to dashboard Cite

show abstract

“…The deduced amino acid sequence of the frm product shared only 33 % identity with that of the flavin reductase gene (dszD) from R. erythropolis IGTS8 (Furuya et al, 2005). Ishii et al (2000) isolated and cloned the gene tdsD encoding the flavin reductase which coupled with the monooxygenases of Paenibacillus sp. A11-2.…”

Section: The Genetics Of Biodesulfurizationmentioning

confidence: 99%

Biocatalytic desulfurization (BDS) of petrodiesel fuels

2008

View full text Add to dashboard Cite

Oil refineries are facing many challenges, including heavier crude oils, increased fuel quality standards, and a need to reduce air pollution emissions. Global society is stepping on the road to zero-sulfur fuel, with only differences in the starting point of sulfur level and rate reduction of sulfur content between different countries. Hydrodesulfurization (HDS) is the most common technology used by refineries to remove sulfur from intermediate streams. However, HDS has several disadvantages, in that it is energy intensive, costly to install and to operate, and does not work well on refractory organosulfur compounds. Recent research has therefore focused on improving HDS catalysts and processes and also on the development of alternative technologies. Among the new technologies one possible approach is biocatalytic desulfurization (BDS). The advantage of BDS is that it can be operated in conditions that require less energy and hydrogen. BDS operates at ambient temperature and pressure with high selectivity, resulting in decreased energy costs, low emission, and no generation of undesirable side products. Over the last two decades several research groups have attempted to isolate bacteria capable of efficient desulfurization of oil fractions. This review examines the developments in our knowledge of the application of bacteria in BDS processes, assesses the technical viability of this technology and examines its future challenges. IntroductionBiotechnology is now accepted as an attractive means of improving the efficiency of many industrial processes, and resolving serious environmental problems. One of the reasons for this is the extraordinary metabolic capability that exists within the bacterial world. Microbial enzymes are capable of biotransforming a wide range of compounds, and the worldwide increase in attention being paid to this concept can be attributed to several factors, including the presence of a wide variety of catabolic enzymes and the ability of many microbial enzymes to transform a broad range of unnatural compounds (xenobiotics) as well as natural compounds. Biotransformation processes have several advantages compared with chemical processes, including: (i) microbial enzyme reactions are often more selective; (ii) biotransformation processes are often more energy-efficient; (iii) microbial enzymes are active under mild conditions; and (iv) microbial enzymes are environment-friendly biocatalysts. Although many biotransformation processes have been described, only a few of these have been used as part of an industrial process. Many opportunities remain in this area.Petroleum biotechnology is based on biotransformation processes. Petroleum microbiology research is advancing on many fronts, spurred on most recently by new knowledge of cellular structure and function gained through molecular and protein engineering techniques, combined with more conventional microbial methods. Current applied research on petroleum microbiology encompasses oil spill remediation, fermenter-and wetland-based hydrocarbon...

show abstract

“…The current maximum SA of 159.0 mmol 2HBP/(kg dry cells·h), in comparison with 135.0 mmol 2HBP/(kg dry cells·h) in our previous report (Yan et al, 2000(Yan et al, ), was et al, 2000, was achieved when R. erythropolis USTB-03 was grown on both nicotinamide of 5 mmol and riboflavin of 25 µmol (Fig.4c). In addition to the enhancement of SA by genetic engineering was widely studied (Ishii et al, 2000;Borole et al, 2002;Nomura et al, 2005), it could also be achieved by the metabolic supplementation using nicotinamide and riboflavin in the culture medium.…”

Section: Effects Of Nicotinamide and Riboflavin On Sa Of R Erythropomentioning

confidence: 99%

“…Previously, high SA of 135.5 mmol 2HBP/(kg dry cells·h) and cell concentration of 37 g dry cells/L of Rhodococcus erythropolis KA2-5-1 were found in a fed-batch fermentation culture, when ethanol as the sole carbon and energy source was maintained at 1.0 g/L under the control of a semiconductor gas sensor (Yan et al, 2000). The genes for biodesulfurization enzymes have been cloned, sequenced and engineered from a variety of microorganisms (Ishii et al, 2000;Borole et al, 2002;Nomura et al, 2005); however, little information was provided on how to increase SA of biodesulfurization through the metabolic promotion of FMNH2 and the production of reduced form of nicotinamide-adenine dinucleotide (NADH) .…”

Section: Introductionmentioning

confidence: 99%

Effects of nicotinamide and riboflavin on the biodesulfurization activity of dibenzothiophene by Rhodococcus erythropolis USTB-03

Yan¹,

Xudong²,

Xu³

et al. 2008

Journal of Environmental Sciences

View full text Add to dashboard Cite

Rhodococcus erythropolis USTB-03 is a promising bacterial strain for the biodesulfurization of dibenzothiophene (DBT) via a sulfurspecific pathway in which DBT is converted to 2-hydroxybiphenyl (2HBP) as an end product. The effects of nicotinamide and riboflavin on the sulfur specific activity (SA) of DBT biodesulfurization by R. erythropolis USTB-03 were investigated. Both nicotinamide and riboflavin were found to enhance the expression of SA, which was not previously reported. When R. erythropolis USTB-03 was grown on a medium containing nicotinamide of 10.0 mmol or riboflavin of 50.0 µmol, SA was raised from 68.0 or so to more than 130 mmol 2HBP/(kg dry cells·h). When R. erythropolis USTB-03 was grown in the presence of both nicotinamide of 5.0 mmol and riboflavin of 25.0 µmol, SA was further increased to 159.0 mmol 2HBP/(kg dry cells·h). It is suggested that the biological synthesis of reduced form of flavin mononucleotide (FMNH2), an essential coenzyme for the activities of biodesulfurization enzyme Dsz C and A, might be enhanced by nicotinamide and riboflavin, which was responsible for the increased SA of R. erythropolis USTB-03.

show abstract

Operon Structure and Functional Analysis of the Genes Encoding Thermophilic Desulfurizing Enzymes of Paenibacillus sp. A11-2

Cited by 94 publications

References 23 publications

A CysB-regulated and σ54-dependent regulator, SfnR, is essential for dimethyl sulfone metabolism of Pseudomonas putida strain DS1

A CysB-regulated and σ54-dependent regulator, SfnR, is essential for dimethyl sulfone metabolism of Pseudomonas putida strain DS1

Biocatalytic desulfurization (BDS) of petrodiesel fuels

Effects of nicotinamide and riboflavin on the biodesulfurization activity of dibenzothiophene by Rhodococcus erythropolis USTB-03

Contact Info

Product

Resources

About