Study of Redox Protein and Enzymes using Theoretical and experimental methods

This thesis investigates the structural dynamics and functional mechanisms of cytochrome P450 aromatase, a key enzyme in estrogen biosynthesis. Using a combination of computational methods, such as molecular dynamics, free energy simulations, and experimental techniques including TIRF microscopy, it explores aromatase's membrane-embedded behaviour, dimerization, and evolutionary adaptations across species. This work reveals the pathways for substrate entry and exit, quantifies the associated energy barriers, and examines how these are influenced by dimerization. By extending the study to CYP17, it offers broader insights into cytochrome P450 dynamics. This integrated approach advances understanding of aromatase’s structure-function relationships and its therapeutic potential.