Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes

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Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes. / Ortiz, Roberto; Matsumura, Hirotoshi; Tasca, Federico; Zahma, Kawah; Samejima, Masahiro; Igarashi, Kiyohiko; Ludwig, Roland; Gorton, Lo.

I: Analytical Chemistry, Vol. 84, Nr. 23, 2012, s. 10315-10323.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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Ortiz, R, Matsumura, H, Tasca, F, Zahma, K, Samejima, M, Igarashi, K, Ludwig, R & Gorton, L 2012, 'Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes', Analytical Chemistry, vol. 84, nr. 23, s. 10315-10323. https://doi.org/10.1021/ac3022899

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Ortiz, Roberto ; Matsumura, Hirotoshi ; Tasca, Federico ; Zahma, Kawah ; Samejima, Masahiro ; Igarashi, Kiyohiko ; Ludwig, Roland ; Gorton, Lo. / Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes. I: Analytical Chemistry. 2012 ; Vol. 84, Nr. 23. s. 10315-10323.

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TY - JOUR

T1 - Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes

AU - Ortiz, Roberto

AU - Matsumura, Hirotoshi

AU - Tasca, Federico

AU - Zahma, Kawah

AU - Samejima, Masahiro

AU - Igarashi, Kiyohiko

AU - Ludwig, Roland

AU - Gorton, Lo

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004), Biochemistry and Structural Biology (S) (000006142)

PY - 2012

Y1 - 2012

N2 - Cellobiose dehydrogenase (CDH) is a monomeric extracellular flavocytochrome composed of a catalytic dehydrogenase domain (DHCDH) containing flavin adenine dinucleotide (FAD), a cytochrome domain (CYTCDH) containing heme b, and a linker region connecting the two domains. In this work, the effect of deglycosylation on the electrochemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (CsCDH) is presented. All the glycosylated and deglycosylated enzymes show direct electron transfer (DET) between the CYTCDH and the electrode. Graphite electrodes modified with deglycosylated PcCDH (dPcCDH) and CsCDH (dCsCDH) have a 40-65% higher I-max value in the presence of substrate than electrodes modified with their glycosylated counterparts. CsCDH trapped under a permselective membrane showed similar changes on gold electrodes protected by a thiol-based self-assembled monolayer (SAM), in contrast to PcCDH for which deglycosylation did not exhibit any different electrocatalytical response on SAM-modified gold electrodes. Glycosylated PcCDH was found to have a 30% bigger hydrodynamic radius than dPcCDH using dynamic light scattering. The basic bioelectrochemistry as well as the bioelectrocatalytic properties are presented.

AB - Cellobiose dehydrogenase (CDH) is a monomeric extracellular flavocytochrome composed of a catalytic dehydrogenase domain (DHCDH) containing flavin adenine dinucleotide (FAD), a cytochrome domain (CYTCDH) containing heme b, and a linker region connecting the two domains. In this work, the effect of deglycosylation on the electrochemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (CsCDH) is presented. All the glycosylated and deglycosylated enzymes show direct electron transfer (DET) between the CYTCDH and the electrode. Graphite electrodes modified with deglycosylated PcCDH (dPcCDH) and CsCDH (dCsCDH) have a 40-65% higher I-max value in the presence of substrate than electrodes modified with their glycosylated counterparts. CsCDH trapped under a permselective membrane showed similar changes on gold electrodes protected by a thiol-based self-assembled monolayer (SAM), in contrast to PcCDH for which deglycosylation did not exhibit any different electrocatalytical response on SAM-modified gold electrodes. Glycosylated PcCDH was found to have a 30% bigger hydrodynamic radius than dPcCDH using dynamic light scattering. The basic bioelectrochemistry as well as the bioelectrocatalytic properties are presented.

U2 - 10.1021/ac3022899

DO - 10.1021/ac3022899

M3 - Article

VL - 84

SP - 10315

EP - 10323

JO - Analytical Chemistry

T2 - Analytical Chemistry

JF - Analytical Chemistry

SN - 1520-6882

IS - 23

ER -