Related Experiment Video
Updated: Jan 15, 2026

Biochemical Measurement of Neonatal Hypoxia
Published on: August 24, 2011
Inhibition of xanthine oxidase by two aldehydes: Inhibitory kinetics, molecular simulation, inhibition mechanism, and
Xiao Wang1, Bingjie Chen1, Songheng Wu1
1Crop Breeding and Cultivation Research Institution, Research Center for Agricultural Products Preservation and Processing, Shanghai Academy of Agricultural Sciences, Shanghai, China.
Abstract:
The inhibitory effects of p-coumaric aldehyde (CA) and p-hydroxybenzaldehyde (HA) on xanthine oxidase (XOD) were systematically evaluated using inhibition kinetics, molecular simulations, mechanistic analyses, and cellular assays. Both compounds were found to act as mixed-type inhibitors, with inhibition primarily mediated by hydrophobic interactions and hydrogen bonding. Molecular dynamics analyses indicated that HA formed more stable hydrogen bonds with XOD, exhibiting consistently lower radius of gyration (Rg) and root mean square deviation (RMSD) values. However, its inhibitory potency was lower than that of CA, potentially due to limited interaction with the catalytic site. Mechanistic investigations revealed that the aldehydes were converted into corresponding acidic products at the molybdenum-pyrimidine center of XOD, with conversion rates and inhibitory effects showing pH dependence. Cellular assays demonstrated that CA and HA reduced uric acid levels and XOD activity within the 25-100 μM range, decreased superoxide anion production, and enhanced total antioxidant capacity. ADMET predictions indicated that these aldehydes possess favorable pharmacokinetic and safety profiles, supporting their potential application as functional ingredients in health foods.
More Related Videos
08:57Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
12:08Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Related Concept Videos
Enzyme Inhibition
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
Oxidations of Aldehydes and Ketones to Carboxylic Acids
Aldehydes readily undergo oxidation in strong oxidizing agents such as potassium permanganate and chromic acid. The oxidation can also be carried out using mild oxidizing agents such as silver oxide. In fact, aldehydes can be easily oxidized...
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...