Comparative modeling of DszC, an enzyme in biodesulfurization, and performing in silico point mutation for increasing tendency to oil

Torktaz, Ibrahim; Etemadifar, Zahra; Derikvand, Peyman

doi:10.6026/97320630008246

Cited by 12 publications

(4 citation statements)

References 11 publications

(12 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From the enzymatic perspective, studies about punctual mutations on enzymes involved in the ''4S'' tend to increase the percentage of BDS (Torktaz et al 2012). An example that may be cited is the species R. erythropolis, which is the most studied bacteria concerning the identification of genes and enzymes involved in this type of biotechnology (Alves et al 2006).…”

Section: Biodesulfurization Currentlymentioning

confidence: 99%

Biodesulfurization: a mini review about the immediate search for the future technology

Boniek

Figueiredo

Santos

et al. 2014

Clean Techn Environ Policy

117

View full text Add to dashboard Cite

A major concern among the environmental agencies includes the emission of sulfurous gas into the environment. Consequently, the oil agencies are in constant search of alternative processes aiming the reduction of sulfur content in fuels. One of the technologies commonly used is the hydrodesulfurization (HDS), but this is a high-cost process that also requires high temperature and pressure. A complementary alternative to HDS is biodesulfurization (BDS) involving the use of specific microorganisms to the removal of sulfur present in the carbon chain, using the oxidation pathway ''4S'', in which there is cleavage of carbon-sulfur bond, and maintaining the calorific value of the organic molecule. The BDS is a low-cost technique when compared with HDS. For this process to occur, activation of specific enzymes is needed, which is controlled by dszABC genes. Therefore, strategies to optimize this process have been of great importance to the oil refineries. For decades, attempts to try to implement BDS in the industry have been made, but difficulties in obtaining satisfactory results led the researchers to seek new knowledge about this bioprocess. The need of more studies concerning implementation on an industrial scale of this process is evident, since this biotechnology is a promising alternative to refineries in the near future.

show abstract

Section: Biodesulfurization Currentlymentioning

confidence: 99%

Biodesulfurization: a mini review about the immediate search for the future technology

Boniek

Figueiredo

Santos

et al. 2014

Clean Techn Environ Policy

117

View full text Add to dashboard Cite

show abstract

“…With increasing petroleum consumption, particularly that of high‐sulfur crude oil, air pollution due to oxysulfides represents a serious concern . The polycyclic aromatic sulfur heterocyclic (PASH) compound dibenzothiophene (DBT) and its derivatives are typical sulfur‐containing compounds found in fossil fuels .…”

Section: Introductionmentioning

confidence: 99%

Structural insights into the stabilization of active, tetrameric DszC by its C-terminus

et al. 2014

View full text Add to dashboard Cite

Dibenzothiophene (DBT) is a typical sulfur-containing compound found in fossil fuels. This compound and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway, which is a well-studied biochemical pathway consisting of four enzymes. DBT monooxygenase (DszC) from Rhodococcus erythropolis is involved in the first step of the 4S pathway. We determined the crystal structure of DszC, which reveals that, in contrast to several homologous proteins, the C-terminus (410-417) of DszC participates in the stabilization of the substrate-binding pocket. Analytical ultracentrifugation analysis and enzymatic assays confirmed that the C-terminus is important for the stabilization of the active conformation of the substrate-binding pocket and the tetrameric state. Therefore, the C-terminus of DszC plays a significant role in the catalytic activity of this enzyme.

show abstract

“…With the ever-growing demand for energy, worldwide crude-oil consumption is continuously rising. The increasing use of high-sulfur crude oil is known to produce petroleum products with a high sulfur content (Torktaz et al, 2012). Combustion of these sulfur-containing fossil fuels has contributed to severe environmental pollution (Li et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary structural analysis of dibenzothiophene monooxygenase (DszC) fromRhodococcus erythropolis

et al. 2013

View full text Add to dashboard Cite

Dibenzothiophene (DBT) and its derivatives are typical sulfur compounds found in fossil fuels. These compounds show resistance to the hydrodesulfurization treatment that is commonly used in industry. Dibenzothiophene monooxygenase (DszC) is responsible for the oxidation of DBT, which is the first and the rate-limiting step in the DBT enzymatic desulfurization 4S pathway. In this study, the crystal structure of DszC from Rhodococcus erythropolis DS-3 is reported. The crystal of native DszC belonged to space group P1, with unitcell parameters a = 96.16, b = 96.27, c = 98.56 Å , = 81.03, = 67.57, = 85.84 . To determine the phase, SAD X-ray diffraction data were collected from a SeMet-derivative DszC crystal, which also belonged to space group P1, with unit-cell parameters a = 95.379, b = 95.167, c = 94.891 Å , = 87.046, = 70.536, = 79.738 . Further structural analysis of DszC is in progress.

show abstract

Comparative modeling of DszC, an enzyme in biodesulfurization, and performing in silico point mutation for increasing tendency to oil

Cited by 12 publications

References 11 publications

Biodesulfurization: a mini review about the immediate search for the future technology

Biodesulfurization: a mini review about the immediate search for the future technology

Structural insights into the stabilization of active, tetrameric DszC by its C-terminus

Crystallization and preliminary structural analysis of dibenzothiophene monooxygenase (DszC) fromRhodococcus erythropolis

Contact Info

Product

Resources

About