Kinetic and structural analysis of redox-reversible artificial imine reductases

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversity of York-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorFederal University of Rio de Janeiro-
Autor(es): dc.creatorMiller, Alex H.-
Autor(es): dc.creatorMartins, Ingrid B.S.-
Autor(es): dc.creatorBlagova, Elena V.-
Autor(es): dc.creatorWilson, Keith S.-
Autor(es): dc.creatorDuhme-Klair, Anne-K.-
Data de aceite: dc.date.accessioned2025-08-21T18:29:52Z-
Data de disponibilização: dc.date.available2025-08-21T18:29:52Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-10-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.jinorgbio.2024.112691-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/299606-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/299606-
Descrição: dc.descriptionThree artificial imine reductases, constructed via supramolecular anchoring utilising FeIII-azotochelin, a natural siderophore, to bind an iridium-containing catalyst to periplasmic siderophore-binding protein (PBP) scaffolds, have previously been synthesised and subjected to catalytic testing. Despite exhibiting high homology and possessing conserved siderophore anchor coordinating residues, the three artificial metalloenzymes (ArMs) displayed significant variability in turnover frequencies (TOFs). To further understand the catalytic properties of these ArMs, their kinetic behaviour was evaluated with respect to the reduction of three cyclic imines: dihydroisoquinoline, harmaline, and papaverine. Kinetic analyses revealed that all examined ArMs adhere to Michaelis-Menten kinetics, with the most pronounced saturation profile observed for the substrate harmaline. Additionally, molecular docking studies suggested varied hydrogen-bonding interactions between substrates and residues within the artificial binding pocket. Pi-stacking and pi-cation interactions were identified for harmaline and papaverine, corroborating the higher affinity of these substrates for the ArMs in comparison to dihydroisoquinoline. Furthermore, it was demonstrated that multiple cavities are capable of accommodating substrates in close proximity to the catalytic centre, thereby rationalising the moderate enantioselectivity conferred by the unmodified scaffolds.-
Descrição: dc.descriptionBiotechnology and Biological Sciences Research Council-
Descrição: dc.descriptionEngineering and Physical Sciences Research Council-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)-
Descrição: dc.descriptionDepartment of Chemistry University of York, York-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Humanities and Exact Sciences São Paulo State University (UNESP), São José do Rio Preto, SP-
Descrição: dc.descriptionBiophysics Institute Carlos Chagas Filho Federal University of Rio de Janeiro, RJ-
Descrição: dc.descriptionStructural Biology Laboratory Department of Chemistry University of York, York-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Humanities and Exact Sciences São Paulo State University (UNESP), São José do Rio Preto, SP-
Idioma: dc.languageen-
Relação: dc.relationJournal of Inorganic Biochemistry-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectArtificial metalloenzymes-
Palavras-chave: dc.subjectKinetics-
Palavras-chave: dc.subjectMichaelis-Menten-
Palavras-chave: dc.subjectMolecular docking-
Título: dc.titleKinetic and structural analysis of redox-reversible artificial imine reductases-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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