Molecular Docking Study on the Interaction of Pesticide Derivatives with Bacterial Enzymes


Özgen A., Terzi R.

IConPB 2025 4 th International Congress on Plant Biology, Denizli, Türkiye, 3 - 06 Eylül 2025, ss.101, (Özet Bildiri)

  • Yayın Türü: Bildiri / Özet Bildiri
  • Basıldığı Şehir: Denizli
  • Basıldığı Ülke: Türkiye
  • Sayfa Sayıları: ss.101
  • İstanbul Gelişim Üniversitesi Adresli: Evet

Özet

Pesticides are toxic chemicals used to eliminate pests that damage agricultural products and increase product yield. As a result of the widespread use of pesticides containing chemicals such as insecticides, herbicides, and fungicides, the soil structure is deteriorated, and usable agricultural land is significantly reduced. At the same time, pesticides mix with groundwater, seep into the sea, and are incorporated into the food chain. They negatively affect terrestrial and aquatic life and have adverse effects on human health. Microorganisms have enzymes that break down these chemicals, and microbial enzymes are promising for the biological degradation of pesticides. While microorganisms themselves can be utilized in this process, microbial enzymes can also be employed in phytoremediation, a biotechnological method for removing pesticide pollution. The genes encoding the enzymes that facilitate the biological degradation of pesticides can be transferred to specific plants to help clean the soil of these chemicals. In this study, the interaction between enzymes from the bacterial species Thermus thermophilus HB27 and Pseudomonas putida and the pesticides acetochlor, malathion, lindane, and vinclozolin was investigated using the molecular docking method. According to the obtained data, it was determined that the oxidoreductase group enzyme belonging to the bacterium Thermus thermophilus HB27 showed binding energies of -7.2 kcal/mol with vinclozolin, -6.3 kcal/mol with acetochlor, -5.3 kcal/mol with malathion and -5.2 kcal/mol with lindane. It was determined that the oxidoreductase group enzyme belonging to the bacterium Pseudomonas putida showed binding energies of -6.8 kcal/mol with vinclozolin, -5.1 kcal/mol with lindane, -5.1 kcal/mol with malathion and -4.8 kcal/mol with acetochlor. The findings show that enzymes from the bacterial species Thermus thermophilus HB27 and Pseudomonas putida exhibit strong interactions with the pesticides acetochlor, malathion, lindane, and vinclozolin.