Abstract

AbstractConcerns about pollinator health and the influence on agricultural ecosystems have developed as a result of pesticide‐caused population declines in honey bees. The research looked at the properties of the SDHA subunit of the enzyme Succinate dehydrogenase, which is important for energy production and mitochondrial function. The goal was to investigate the structural and functional characteristics of SDHA in several Apis bee species, as well as how pesticides can limit its activity. In silico analyses were conducted to understand the structural characteristics of the SDHA subunit, assess evolutionary conservation, analyze deformation energy, and investigate potential pesticide binding. Thirteen pesticides were subjected to molecular docking studies with the Apis SDHA subunit. The study revealed the stability and conserved nature of the SDHA subunit across different Apis sp. Deformation energy analysis highlighted regions of local flexibility, particularly in the active site and interdomain interfaces. Molecular docking analysis indicated that pesticides such as Carboxin, Clothianidin, and Dithianon potentially interfere with FAD binding, while Fipronil and Sulfoxaflor may disrupt both FAD and dicarboxylate binding. This research sheds light on pesticides′ probable inhibitory effects on SDH, a vital enzyme in honey bee energy production and mitochondrial function. The findings highlight the importance of stringent pesticide controls and long‐term pest management measures to protect pollinator numbers and ecosystem health.

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