Publication detail

In-silico studies of Cu-Zn superoxide dismutase enzyme from helianthus annuus with polycyclic aromatic hydrocarbons to find out insight into its phytoremediation capabilities

ROY, S. SONI, G. SHARMA, A. PROVAZNÍK, I.

Original Title

In-silico studies of Cu-Zn superoxide dismutase enzyme from helianthus annuus with polycyclic aromatic hydrocarbons to find out insight into its phytoremediation capabilities

English Title

In-silico studies of Cu-Zn superoxide dismutase enzyme from helianthus annuus with polycyclic aromatic hydrocarbons to find out insight into its phytoremediation capabilities

Type

conference paper

Language

en

Original Abstract

Cu-Zn superoxide dismutase is an enzyme that is reported to detoxify heavy metals and thus aid in phytoremediation. In this study an effort has been made to explore the wide potential of Cu-Zn superoxide dismutase enzyme found in Helianthus annuus for its capability to degrade pollutants of several industries which are mainly polycyclic aromatic hydrocarbons. It includes pollutants from iron, steel, rubber, stone and glass industries. Comparative Genornics approach was employed in order to deduce the similarity between Aldehyde Keto Reductase (AKRs) related ESTs and gene corresponding to Cu-Zn superoxide dismutase (SOD1) in Helianthus annuus. This was followed by modeling of Cu-Zn superoxide dismutase protein. Motif and profile studies correlated the findings. Physico-chemical and functional characterization of the modeled protein was performed. The modeled protein is thermostable over wide range of temperatures and also has high aliphatic index. For molecular docking, a set of pollutants were selected from five different industries. The data were obtained from Environment Protection Agency (EPA) for iron, steel, rubber, stone and glass industries. Protein-ligand docking was carried out using Discovery Studio. Dibenzofuran, anthracene, Butyl benzyl phthalate, Tetrabromobisphenol, Mercaptobenzothiazole, Flumeturon and phenyl isocyanate dimer from different industries showed better binding capability with the Cu-Zn Superoxide Dismutase protein. These findings needs to be further tested in the field condition for its validation. These studies may open new avenues for utilizing the medicinal plants and their detoxifying properties for remediation of hazardous pollutants.

English abstract

Cu-Zn superoxide dismutase is an enzyme that is reported to detoxify heavy metals and thus aid in phytoremediation. In this study an effort has been made to explore the wide potential of Cu-Zn superoxide dismutase enzyme found in Helianthus annuus for its capability to degrade pollutants of several industries which are mainly polycyclic aromatic hydrocarbons. It includes pollutants from iron, steel, rubber, stone and glass industries. Comparative Genornics approach was employed in order to deduce the similarity between Aldehyde Keto Reductase (AKRs) related ESTs and gene corresponding to Cu-Zn superoxide dismutase (SOD1) in Helianthus annuus. This was followed by modeling of Cu-Zn superoxide dismutase protein. Motif and profile studies correlated the findings. Physico-chemical and functional characterization of the modeled protein was performed. The modeled protein is thermostable over wide range of temperatures and also has high aliphatic index. For molecular docking, a set of pollutants were selected from five different industries. The data were obtained from Environment Protection Agency (EPA) for iron, steel, rubber, stone and glass industries. Protein-ligand docking was carried out using Discovery Studio. Dibenzofuran, anthracene, Butyl benzyl phthalate, Tetrabromobisphenol, Mercaptobenzothiazole, Flumeturon and phenyl isocyanate dimer from different industries showed better binding capability with the Cu-Zn Superoxide Dismutase protein. These findings needs to be further tested in the field condition for its validation. These studies may open new avenues for utilizing the medicinal plants and their detoxifying properties for remediation of hazardous pollutants.

Keywords

Helianthus Annuus, Phytoremediation, Polycyclic Hydrocarbons, Molecular Docking

RIV year

2014

Released

30.09.2014

Publisher

International Phytotechnology Society

Location

Crete, Greece

ISBN

978-960-6865-81-7

Book

11th International Phytotechnologies Conference

Edition

11

Pages from

189

Pages to

189

Pages count

1

BibTex


@inproceedings{BUT110436,
  author="Sudeep {Roy} and Garima {Soni} and Ashok {Sharma} and Ivo {Provazník}",
  title="In-silico studies of Cu-Zn superoxide dismutase enzyme from helianthus annuus with polycyclic aromatic hydrocarbons to find out insight into its phytoremediation capabilities",
  annote="Cu-Zn superoxide dismutase is an enzyme that is reported to detoxify heavy metals and thus aid in phytoremediation. In this study an effort has been made to explore the wide potential of Cu-Zn superoxide dismutase enzyme found in Helianthus annuus for its capability to degrade pollutants of several industries which are mainly polycyclic aromatic hydrocarbons. It includes pollutants from iron, steel, rubber, stone and glass industries. Comparative Genornics approach was employed in order to deduce the similarity between Aldehyde Keto Reductase (AKRs) related ESTs and gene corresponding to Cu-Zn superoxide dismutase (SOD1) in Helianthus annuus. This was followed by modeling of Cu-Zn superoxide dismutase protein. Motif and profile studies correlated the findings. Physico-chemical and functional characterization of the modeled protein was performed. The modeled protein is thermostable over wide range of temperatures and also has high aliphatic index. For molecular docking, a set of pollutants were selected from five different industries. The data were obtained from Environment Protection Agency (EPA) for iron, steel, rubber, stone and glass industries. Protein-ligand docking was carried out using Discovery Studio. Dibenzofuran, anthracene, Butyl benzyl phthalate, Tetrabromobisphenol, Mercaptobenzothiazole, Flumeturon and phenyl isocyanate dimer from different industries showed better binding capability with the Cu-Zn Superoxide Dismutase protein. These findings needs to be further tested in the field condition for its validation. These studies may open new avenues for utilizing the medicinal plants and their detoxifying properties for remediation of hazardous pollutants.",
  address="International Phytotechnology Society",
  booktitle="11th International Phytotechnologies Conference",
  chapter="110436",
  edition="11",
  howpublished="print",
  institution="International Phytotechnology Society",
  year="2014",
  month="september",
  pages="189--189",
  publisher="International Phytotechnology Society",
  type="conference paper"
}