ArticleScientific reports2017
Computational insights for the hydride transfer and distinctive roles of key residues in cholesterol oxidase.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 19 citations in OpenAlex.
- Experimental and In Silico Studies on the Development of an Electrochemical Biosensor for the Quantification of HBiosensors · 2025Article
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- Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase.PloS one · 2023Article
- Computational Analysis of the Nicotine Oxidoreductase Mechanism by the ONIOM Method.ACS omega · 2021Article
- Mechanistic study of L-6-hydroxynicotine oxidase by DFT and ONIOM methods.Journal of molecular modeling · 2021Article
- Lignin peroxidase ligand access channel dysfunction in the presence of atrazine.Scientific reports · 2018Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cholesterol oxidase (ChOx), a member of the glucose-methanol-choline (GMC) family, catalyzes the oxidation of the substrate via a hydride transfer mechanism and concomitant reduction of the FAD cofactor. Unlike other GMC enzymes, the conserved His447 is not the catalytic base that deprotonates the substrate in ChOx. Our QM/MM MD simulations indicate that the Glu361 residue acts as a catalytic base facilitating the hydride transfer from the substrate to the cofactor. We find that two rationally chosen point mutations (His447Gln and His447Asn) cause notable decreases in the catalytic activity. The binding free energy calculations show that the Glu361 and His447 residues are important in substrate binding. We also performed high-level double-hybrid density functional theory simulations using small model systems, which support the QM/MM MD results. Our work provides a basis for unraveling the substrate oxidation mechanism in GMC enzymes in which the conserved histidine does not act as a base.
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