TORBENSEN, Kristian; PATEL, Anisha; ANNE, Agnès; DEMAILLE, Christophe; BATAILLE, Laure; MICHON, Thierry; GRELET, Eric

doi:10.1021/acscatal.9b01263

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TORBENSEN, Kristian
Laboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]

PATEL, Anisha
Laboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]

ANNE, Agnès
Laboratoire d'Electrochimie Moléculaire [LEM (UMR_7591)]

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Article de revue

Ce document a été publié dans

ACS Catalysis. 2019-05-15, vol. 9, n° 6, p. 5783-5796

American Chemical Society

Résumé en anglais

A virus-based nanostructuring strategy is proposed for improving the catalytic performance of integrated redox enzyme electrodes. Random arrays of adsorbed filamentous fd bacteriophage particles, used as scaffolds, are assembled onto gold electrode surfaces. The viral particles are endowed with functionally coupled enzymatic and redox properties, by the sequential immunological assembly of quinoprotein glucose dehydrogenase conjugated antibodies and ferrocene PEGylated antibodies on their protein shell. The resulting virus-scaffolded enzyme/redox mediator integrated system displays a large enhancement in the catalytic current generated per enzyme molecule (i.e., in enzymatic turnover) as compared with nonscaffolded integrated glucose oxidizing enzyme electrodes. The mechanism underlying the observed scaffolding-induced catalytic enhancement is deciphered. Confinement of the mediator on the viral scaffold enables fast electron transport rate and shifts the enzyme behavior into its most effective cooperative kinetic mode.< Réduire

Mots clés en anglais

bioelectrocatalytic viral particles

enzyme

bioelectrocatalysis

pyrroloquinoline quinone-dependent glucose dehydrogenase

nanocarriers

bioscaffolding

DOI

http://dx.doi.org/10.1021/acscatal.9b01263

Project ANR

Imagerie électrochimique fonctionnelle de systèmes enzymatiques multi-composants organisés sur des virus nano-gabarits - ANR-14-CE09-0009

Origine

Importé de hal

Unités de recherche

Biologie du Fruit & Pathologie (BFP) - UMR 1332