Cargando…
Computational insights for the hydride transfer and distinctive roles of key residues in cholesterol oxidase
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 s...
Autores principales: | Yu, Li-Juan, Golden, Emily, Chen, Nanhao, Zhao, Yuan, Vrielink, Alice, Karton, Amir |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5722936/ https://www.ncbi.nlm.nih.gov/pubmed/29222497 http://dx.doi.org/10.1038/s41598-017-17503-x |
Ejemplares similares
-
An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase
por: Golden, Emily, et al.
Publicado: (2017) -
Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase
por: Yildiz, Ibrahim
Publicado: (2023) -
Empirical Valence Bond Simulations Suggest a Direct
Hydride Transfer Mechanism for Human Diamine Oxidase
por: Maršavelski, Aleksandra, et al.
Publicado: (2018) -
Mechanistic basis for tuning iridium hydride photochemistry from H(2) evolution to hydride transfer hydrodechlorination
por: Barrett, Seth M., et al.
Publicado: (2020) -
Metallated dihydropyridinates: prospects in hydride transfer and (electro)catalysis
por: Parsons, Leo W. T., et al.
Publicado: (2023)