Insight into the binding characteristics of rutin and alcohol dehydrogenase: Based on the biochemical method, spectroscopic experimental and molecular model

Alcohol dehydrogenase (ADH) is a crucial enzyme in the alcohol metabolism pathway. Its activity is associated with the development of alcohol-relative diseases. Rutin is a kind of widely distributed dietary flavonoids, which have the ability to resist alcohol-induced liver injury. Here, the role of rutin on alcohol metabolism was investigated via the methods of biochemistry, spectroscopy and computer simulation. The experiment results demonstrated that rutin entered into the position of coenzyme (NAD) on ADH and formed a binary complex, which of process activated the catalyze activity of ADH in a concentration dependent manner. The combination of rutin on ADH induced microenvironmental variations as well as secondary structural change of ADH, where the level of α-helix reduced yet β-sheet raised. The values of ∆H and ∆S suggested that H-bonds and van der Waals force occupied vital roles in the stabilization of ADH-rutin complex. Furthermore, molecular docking results further confirmed that the H-bonds between the hydroxyl groups on the benzene rings of rutin and surrounding amino acid were beneficial to maintain the stability of complex. Particularly, the van der Waals force and π-alkyl between rutin and Val residues may be the main reason for activation of ADH activity.