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Enzymatic Activity of Individual Bioelectrocatalytic Viral Nanoparticles: Dependence of Catalysis on the Viral Scaffold and its Length

hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorPAIVA, Telmo
hal.structure.identifierUniversität Stuttgart [Stuttgart]
dc.contributor.authorSCHNEIDER, Angela
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBATAILLE, Laure
hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorCHOVIN, Arnaud
hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorANNE, Agnès
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMICHON, Thierry
hal.structure.identifierUniversität Stuttgart [Stuttgart]
dc.contributor.authorWEGE, Christina
hal.structure.identifierLaboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]
dc.contributor.authorDEMAILLE, Christophe
dc.date.issued2022
dc.identifier.issn2040-3364
dc.description.abstractEnThe enzymatic activity of tobacco mosaic virus (TMV) nanorod particles decorated with an integrated electro-catalytic system, comprising the quinoprotein glucose-dehydrogenase (PQQ-GDH) enzyme and ferrocenylated PEG chains as redox mediators, is probed at the individual virion scale by scanning electrochemical atomic force microscopy (AFM-SECM). A marked dependence of the catalytic activity on the particle length is observed. This finding can be explained by electron propagation along the viral backbone, resulting from electron exchange between ferrocene moieties, coupled with enzymatic catalysis. Thus, the use of a simple 1D diffusion/reaction model allows the determination of the kinetic parameters of the virus-supported enzyme. Comparative analysis of the catalytic behavior of the Fc-PEG/PQQ-GDH system assembled on two differing viral scaffolds, TMV (this work) and bacteriophage-fd (previous work), reveals two distinct kinetic effects of scaffolding: An enhancement of catalysis that does not depend on the virus type and a modulation of substrate inhibition that depends on the virus type. AFM-SECM detection of the enzymatic activity of a few tens of PQQ-GDH molecules, decorating a 40 nm-long viral domain, is also demonstrated, a record in terms of the lowest number of enzyme molecules interrogated by an electrochemical imaging technique.
dc.language.isoen
dc.publisherRoyal Society of Chemistry
dc.subject.entobacco mosaic virus
dc.subject.envirus like particles
dc.subject.enVLPs
dc.subject.ennanotechnology
dc.subject.encatalysis
dc.subject.enenzyme
dc.subject.enAFM-SECM
dc.title.enEnzymatic Activity of Individual Bioelectrocatalytic Viral Nanoparticles: Dependence of Catalysis on the Viral Scaffold and its Length
dc.typeArticle de revue
dc.identifier.doi10.1039/D1NR07445H
dc.subject.halChimie/Catalyse
dc.subject.halChimie/Chimie théorique et/ou physique
dc.subject.halSciences du Vivant [q-bio]/Biotechnologies
bordeaux.journalNanoscale
bordeaux.page875-889
bordeaux.volume14
bordeaux.issue3
bordeaux.peerReviewedoui
hal.identifierhal-03500861
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-03500861v1
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