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hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorKASSEM, Racha
hal.structure.identifierInstitut de Biologie Moléculaire des Plantes [IBMP]
dc.contributor.authorCOUSIN, Anne
hal.structure.identifierInstitut de Biologie Moléculaire des Plantes [IBMP]
dc.contributor.authorCLESSE, Daniel
hal.structure.identifierInstitut de Biologie Moléculaire des Plantes [IBMP]
dc.contributor.authorPOIGNAVENT, Vianney
hal.structure.identifierInstitut de Biologie Moléculaire des Plantes [IBMP]
dc.contributor.authorTROLET, Adrien
hal.structure.identifierInstitut de Biologie Moléculaire des Plantes [IBMP]
dc.contributor.authorRITZENTHALER, Christophe
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMICHON, Thierry
hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorCHOVIN, Arnaud
hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorDEMAILLE, Christophe
dc.date.issued2024-02
dc.identifier.issn1567-5394
dc.description.abstractEnIcosahedral, 30 nm diameter, grapevine fanleaf virus (GFLV) virus particles are adsorbed onto electrodes and used as nanoscaffolds for the assembly of an integrated glucose oxidizing system, comprising the enzyme pyrroloquinoline quinone-glucose dehydrogenase (PQQ-GDH) and ferrocenylated polyethylene glycol chains (Fc-PEG) as a redox cosubstrate. Two different GFLVspecific nanobodies, either fused to the enzyme, or chemically conjugated to Fc-PEG, are used for the regio-selective immunodecoration of the viral particles. A comprehensive kinetic characterization of the enzymatic function of the particles, initially decorated with the enzyme alone shows that simple immobilization on the GFLV capsid has no effect on the kinetic scheme of the enzyme, nor on its catalytic activity. However, we find that co-immobilization of the enzyme and the Fc-PEG cosubtrate on GFLV does induce enzymatic enhancement, by promoting cooperativity between the two subunits of the homodimeric enzyme, via "synchronization" of their redox state. A decrease in inhibition of the enzyme by its substrate (glucose) is also observed.
dc.language.isoen
dc.publisherElsevier
dc.subject.enPQQ-GDH Bioscaffolding Nanoparticle enhanced bioelectrocatalysis Viral nanotechnology
dc.subject.enPQQ-GDH
dc.subject.enBioscaffolding
dc.subject.enNanoparticle enhanced bioelectrocatalysis
dc.subject.enViral nanotechnology
dc.title.enNanobody-guided redox and enzymatic functionalization of icosahedral virus particles for enhanced bioelectrocatalysis
dc.typeArticle de revue
dc.identifier.doi10.1016/j.bioelechem.2023.108570
dc.subject.halChimie
bordeaux.journalBioelectrochemistry
bordeaux.page108570
bordeaux.volume155
bordeaux.peerReviewedoui
hal.identifierhal-04284453
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-04284453v1
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