Wiring of heme enzymes by methylene-blue labeled dendrimers

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Standard

Wiring of heme enzymes by methylene-blue labeled dendrimers. / Álvarez-Martos, Isabel; Shahdost-fard, Faezeh ; Ferapontova, Elena.

I: Electrochimica Acta, Bind 249, 20.09.2017, s. 206-215.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Álvarez-Martos, I, Shahdost-fard, F & Ferapontova, E 2017, 'Wiring of heme enzymes by methylene-blue labeled dendrimers', Electrochimica Acta, bind 249, s. 206-215. https://doi.org/10.1016/j.electacta.2017.07.161

APA

Álvarez-Martos, I., Shahdost-fard, F., & Ferapontova, E. (2017). Wiring of heme enzymes by methylene-blue labeled dendrimers. Electrochimica Acta, 249, 206-215. https://doi.org/10.1016/j.electacta.2017.07.161

CBE

MLA

Álvarez-Martos, Isabel, Faezeh Shahdost-fard, og Elena Ferapontova. "Wiring of heme enzymes by methylene-blue labeled dendrimers". Electrochimica Acta. 2017, 249. 206-215. https://doi.org/10.1016/j.electacta.2017.07.161

Vancouver

Álvarez-Martos I, Shahdost-fard F, Ferapontova E. Wiring of heme enzymes by methylene-blue labeled dendrimers. Electrochimica Acta. 2017 sep 20;249:206-215. https://doi.org/10.1016/j.electacta.2017.07.161

Author

Álvarez-Martos, Isabel ; Shahdost-fard, Faezeh ; Ferapontova, Elena. / Wiring of heme enzymes by methylene-blue labeled dendrimers. I: Electrochimica Acta. 2017 ; Bind 249. s. 206-215.

Bibtex

@article{51d301c786be4cdb85ca9610bb41c306,
title = "Wiring of heme enzymes by methylene-blue labeled dendrimers",
abstract = "Redox-modified branched 3D dendrimeric nanostructures may be considered as perspective wires for electrical connection between redox enzymes and electrodes. Here, we studied electron transfer (ET) reactions and bioelectrocatalysis of heme-containing horseradish peroxidase (HRP) and heme- and molibdopterin-containing sulfite oxidase (SOx), wired to gold by the methylene blue (MB)-labeled polyamidoamine (PAMAM) dendrimers. The enzymes{\textquoteright} electrochemical transformation and bioelectrocatalyticfunction could be followed at both unlabeled and MB-labeled dendrimer-modified electrodes with the formal redox potentials of the heme centers being at 341 mV for HRP and 185 mV for SOx. In contrast to the HRP-dendrimer and HRP-MB-dendrimer systems, which demonstrated very close bioelectrocatalytic patterns, multicofactor SOx wired to MB-dendrimer showed a bioelectrocatalysis superior to that based on direct ET reaction. This can be correlated with a statistically larger number of positively charged MB sites on the dendrimer surface able to electrically connect the negatively charged heme domain of SOx and the electrode. In this perspective, redox-labeled dendrimers appear to be useful tools for wiring, optimization of bioelectrocatalysis of complex intermembrane and, possibly, membrane enzymes.",
keywords = "BIOELECTROCATALYSIS, Dendrimers, Methylene blue , Horseradish Peroxidase, SULFITE OXIDASE",
author = "Isabel {\'A}lvarez-Martos and Faezeh Shahdost-fard and Elena Ferapontova",
year = "2017",
month = sep,
day = "20",
doi = "10.1016/j.electacta.2017.07.161",
language = "English",
volume = "249",
pages = "206--215",
journal = "Electrochimica Acta",
issn = "0013-4686",
publisher = "Pergamon Press",

}

RIS

TY - JOUR

T1 - Wiring of heme enzymes by methylene-blue labeled dendrimers

AU - Álvarez-Martos, Isabel

AU - Shahdost-fard, Faezeh

AU - Ferapontova, Elena

PY - 2017/9/20

Y1 - 2017/9/20

N2 - Redox-modified branched 3D dendrimeric nanostructures may be considered as perspective wires for electrical connection between redox enzymes and electrodes. Here, we studied electron transfer (ET) reactions and bioelectrocatalysis of heme-containing horseradish peroxidase (HRP) and heme- and molibdopterin-containing sulfite oxidase (SOx), wired to gold by the methylene blue (MB)-labeled polyamidoamine (PAMAM) dendrimers. The enzymes’ electrochemical transformation and bioelectrocatalyticfunction could be followed at both unlabeled and MB-labeled dendrimer-modified electrodes with the formal redox potentials of the heme centers being at 341 mV for HRP and 185 mV for SOx. In contrast to the HRP-dendrimer and HRP-MB-dendrimer systems, which demonstrated very close bioelectrocatalytic patterns, multicofactor SOx wired to MB-dendrimer showed a bioelectrocatalysis superior to that based on direct ET reaction. This can be correlated with a statistically larger number of positively charged MB sites on the dendrimer surface able to electrically connect the negatively charged heme domain of SOx and the electrode. In this perspective, redox-labeled dendrimers appear to be useful tools for wiring, optimization of bioelectrocatalysis of complex intermembrane and, possibly, membrane enzymes.

AB - Redox-modified branched 3D dendrimeric nanostructures may be considered as perspective wires for electrical connection between redox enzymes and electrodes. Here, we studied electron transfer (ET) reactions and bioelectrocatalysis of heme-containing horseradish peroxidase (HRP) and heme- and molibdopterin-containing sulfite oxidase (SOx), wired to gold by the methylene blue (MB)-labeled polyamidoamine (PAMAM) dendrimers. The enzymes’ electrochemical transformation and bioelectrocatalyticfunction could be followed at both unlabeled and MB-labeled dendrimer-modified electrodes with the formal redox potentials of the heme centers being at 341 mV for HRP and 185 mV for SOx. In contrast to the HRP-dendrimer and HRP-MB-dendrimer systems, which demonstrated very close bioelectrocatalytic patterns, multicofactor SOx wired to MB-dendrimer showed a bioelectrocatalysis superior to that based on direct ET reaction. This can be correlated with a statistically larger number of positively charged MB sites on the dendrimer surface able to electrically connect the negatively charged heme domain of SOx and the electrode. In this perspective, redox-labeled dendrimers appear to be useful tools for wiring, optimization of bioelectrocatalysis of complex intermembrane and, possibly, membrane enzymes.

KW - BIOELECTROCATALYSIS

KW - Dendrimers

KW - Methylene blue

KW - Horseradish Peroxidase

KW - SULFITE OXIDASE

U2 - 10.1016/j.electacta.2017.07.161

DO - 10.1016/j.electacta.2017.07.161

M3 - Journal article

VL - 249

SP - 206

EP - 215

JO - Electrochimica Acta

JF - Electrochimica Acta

SN - 0013-4686

ER -