Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles

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Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles. / B. Jensen, Uffe ; Mohammad-Beigi, Hossein; Shipovskov, Stepan; Sutherland, Duncan S; Ferapontova, Elena.

In: ChemElectroChem, Vol. 6, No. 19, 01.10.2019, p. 5032-5040.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

B. Jensen, U, Mohammad-Beigi, H, Shipovskov, S, Sutherland, DS & Ferapontova, E 2019, 'Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles', ChemElectroChem, vol. 6, no. 19, pp. 5032-5040. https://doi.org/10.1002/celc.201901066

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Author

B. Jensen, Uffe ; Mohammad-Beigi, Hossein ; Shipovskov, Stepan ; Sutherland, Duncan S ; Ferapontova, Elena. / Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles. In: ChemElectroChem. 2019 ; Vol. 6, No. 19. pp. 5032-5040.

Bibtex

@article{7b39320a319b436a8b0da1701b68172b,
title = "Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles",
abstract = "Protein-nanoparticle (NP) interactions offer a powerful tool to modulate enzymatic activity and activate biocatalysis. However, strong scattering effects may complicate conventional spectrophotometric studies of NP-assisted biocatalysis. Here, bioelectrocatalytic oxidation of cellobiose by the Humicola insolens cellobiose dehydrogenase (CDH) was electrochemically interrogated with two redox mediators, ferricyanide and cytochrome c, and two types of carbon NPs (CNPs), unmodified (CNP) and negatively charged 4-sulfophenyl-modified (CNP-) ones. We show that both CNPs activate the bioelectrocatalytic oxidation of cellobiose and improve the enzymatic specificity reflected in the k f/K M relationship of 6680 (no CNPs), 15500 (CNP-) and 10444 M −1 s −1 (CNP) shown for ferricyanide-mediated and 1262 (no CNPs), 3630 (CNP-), and 6375 M −1 s −1 (CNP) for cytochrome c-mediated reactions. The bioelectrocatalysis activation by CNPs apparently results from the interfacial/conformational regulation of the CDH activity and the CDH-electron acceptor reactivity, which may also be the case of other nanomaterials such as frequently used in bioelectrochemistry carbon nanotubes. ",
keywords = "bioelectrocatalysis, carbon nanoparticles, cellobiose dehydrogenase, cytochrome c, enzyme activation, ferricyanide",
author = "{B. Jensen}, Uffe and Hossein Mohammad-Beigi and Stepan Shipovskov and Sutherland, {Duncan S} and Elena Ferapontova",
year = "2019",
month = oct,
day = "1",
doi = "10.1002/celc.201901066",
language = "English",
volume = "6",
pages = "5032--5040",
journal = "ChemElectroChem",
issn = "2196-0216",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "19",

}

RIS

TY - JOUR

T1 - Activation of Cellobiose Dehydrogenase Bioelectrocatalysis by Carbon Nanoparticles

AU - B. Jensen, Uffe

AU - Mohammad-Beigi, Hossein

AU - Shipovskov, Stepan

AU - Sutherland, Duncan S

AU - Ferapontova, Elena

PY - 2019/10/1

Y1 - 2019/10/1

N2 - Protein-nanoparticle (NP) interactions offer a powerful tool to modulate enzymatic activity and activate biocatalysis. However, strong scattering effects may complicate conventional spectrophotometric studies of NP-assisted biocatalysis. Here, bioelectrocatalytic oxidation of cellobiose by the Humicola insolens cellobiose dehydrogenase (CDH) was electrochemically interrogated with two redox mediators, ferricyanide and cytochrome c, and two types of carbon NPs (CNPs), unmodified (CNP) and negatively charged 4-sulfophenyl-modified (CNP-) ones. We show that both CNPs activate the bioelectrocatalytic oxidation of cellobiose and improve the enzymatic specificity reflected in the k f/K M relationship of 6680 (no CNPs), 15500 (CNP-) and 10444 M −1 s −1 (CNP) shown for ferricyanide-mediated and 1262 (no CNPs), 3630 (CNP-), and 6375 M −1 s −1 (CNP) for cytochrome c-mediated reactions. The bioelectrocatalysis activation by CNPs apparently results from the interfacial/conformational regulation of the CDH activity and the CDH-electron acceptor reactivity, which may also be the case of other nanomaterials such as frequently used in bioelectrochemistry carbon nanotubes.

AB - Protein-nanoparticle (NP) interactions offer a powerful tool to modulate enzymatic activity and activate biocatalysis. However, strong scattering effects may complicate conventional spectrophotometric studies of NP-assisted biocatalysis. Here, bioelectrocatalytic oxidation of cellobiose by the Humicola insolens cellobiose dehydrogenase (CDH) was electrochemically interrogated with two redox mediators, ferricyanide and cytochrome c, and two types of carbon NPs (CNPs), unmodified (CNP) and negatively charged 4-sulfophenyl-modified (CNP-) ones. We show that both CNPs activate the bioelectrocatalytic oxidation of cellobiose and improve the enzymatic specificity reflected in the k f/K M relationship of 6680 (no CNPs), 15500 (CNP-) and 10444 M −1 s −1 (CNP) shown for ferricyanide-mediated and 1262 (no CNPs), 3630 (CNP-), and 6375 M −1 s −1 (CNP) for cytochrome c-mediated reactions. The bioelectrocatalysis activation by CNPs apparently results from the interfacial/conformational regulation of the CDH activity and the CDH-electron acceptor reactivity, which may also be the case of other nanomaterials such as frequently used in bioelectrochemistry carbon nanotubes.

KW - bioelectrocatalysis

KW - carbon nanoparticles

KW - cellobiose dehydrogenase

KW - cytochrome c

KW - enzyme activation

KW - ferricyanide

U2 - 10.1002/celc.201901066

DO - 10.1002/celc.201901066

M3 - Journal article

VL - 6

SP - 5032

EP - 5040

JO - ChemElectroChem

JF - ChemElectroChem

SN - 2196-0216

IS - 19

ER -