The role of the active site lysine residue on FAD reduction by NADPH in glutathione reductase.

Enzyme catalysis Flavoproteins Hydride transfer QM/MM

Journal

Computational biology and chemistry

ISSN: 1476-928X

Titre abrégé: Comput Biol Chem

Pays: England

ID NLM: 101157394

Informations de publication

Date de publication:
16 Apr 2024

Historique:

received: 22 11 2023

revised: 01 04 2024

accepted: 11 04 2024

medline: 29 4 2024

pubmed: 29 4 2024

entrez: 28 4 2024

Statut: aheadofprint

Résumé

Glutathione reductase (GR) is a two dinucleotide binding domain flavoprotein (tDBDF) that catalyzes the reduction of glutathione disulfide to glutathione coupled to the oxidation of NADPH to NADP

Identifiants

DOI: 10.1016/j.compbiolchem.2024.108075 PMID: 38678729

pubmed: 38678729

pii: S1476-9271(24)00063-X

doi: 10.1016/j.compbiolchem.2024.108075

pii:

doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

Pagination

108075

Informations de copyright

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.