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Title: pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase

Abstract

A pyranose dehydrogenase from Coprinopsis cinerea (CcPDH) is an extracellular quinohemoeprotein, which consists a b-type cytochrome domain, a pyrroloquinoline-quinone (PQQ) domain, and a family 1-type carbohydrate-binding module. The electron transfer reaction of CcPDH was studied using some electron acceptors and a carbon electrode at various pH levels. Phenazine methosulfate (PMS) reacted directly at the PQQ domain, whereas cytochrome c (cyt c) reacted via the cytochrome domain of intact CcPDH. Thus, electrons are transferred from reduced PQQ in the catalytic domain of CcPDH to heme b in the N-terminal cytochrome domain, which acts as a built-in mediator and transfers electron to a heterogenous electron transfer protein. The optimal pH values of the PMS reduction (pH 6.5) and the cyt c reduction (pH 8.5) differ. The catalytic currents for the oxidation of L-fucose were observed within a range of pH 4.5 to 11. Bioelectrocatalysis of CcPDH based on direct electron transfer demonstrated that the pH profile of the biocatalytic current was similar to the reduction activity of cyt c characters. - Highlights: • pH dependencies of activity were different for the reduction of cyt c and DCPIP. • DET-based bioelectrocatalysis of CcPDH was observed. • The similar pH-dependent profile was found withmore » cyt c and electrode. • The present results suggested that IET reaction of CcPDH shows pH dependence.« less

Authors:
 [1]; ;  [2];  [3]; ;  [2];  [1];  [1]
  1. Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588 (Japan)
  2. Department of Biomaterial Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657 (Japan)
  3. Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Fuchu, Tokyo 183-8509 (Japan)
Publication Date:
OSTI Identifier:
22606167
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 477; Journal Issue: 3; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 60 APPLIED LIFE SCIENCES; ADENINES; BENZOQUINONES; BINDING ENERGY; CELLOBIOSE; ELECTRODES; ELECTRON TRANSFER; ENZYMES; HEME; HEXOSES; ISOALLOXAZINES; OXIDATION; PH VALUE; PHENAZINE; TRANSFER REACTIONS

Citation Formats

Takeda, Kouta, Matsumura, Hirotoshi, Ishida, Takuya, Yoshida, Makoto, Igarashi, Kiyohiko, Samejima, Masahiro, Ohno, Hiroyuki, and Nakamura, Nobuhumi. pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase. United States: N. p., 2016. Web. doi:10.1016/J.BBRC.2016.06.096.
Takeda, Kouta, Matsumura, Hirotoshi, Ishida, Takuya, Yoshida, Makoto, Igarashi, Kiyohiko, Samejima, Masahiro, Ohno, Hiroyuki, & Nakamura, Nobuhumi. pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase. United States. https://doi.org/10.1016/J.BBRC.2016.06.096
Takeda, Kouta, Matsumura, Hirotoshi, Ishida, Takuya, Yoshida, Makoto, Igarashi, Kiyohiko, Samejima, Masahiro, Ohno, Hiroyuki, and Nakamura, Nobuhumi. Fri . "pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase". United States. https://doi.org/10.1016/J.BBRC.2016.06.096.
@article{osti_22606167,
title = {pH-dependent electron transfer reaction and direct bioelectrocatalysis of the quinohemoprotein pyranose dehydrogenase},
author = {Takeda, Kouta and Matsumura, Hirotoshi and Ishida, Takuya and Yoshida, Makoto and Igarashi, Kiyohiko and Samejima, Masahiro and Ohno, Hiroyuki and Nakamura, Nobuhumi},
abstractNote = {A pyranose dehydrogenase from Coprinopsis cinerea (CcPDH) is an extracellular quinohemoeprotein, which consists a b-type cytochrome domain, a pyrroloquinoline-quinone (PQQ) domain, and a family 1-type carbohydrate-binding module. The electron transfer reaction of CcPDH was studied using some electron acceptors and a carbon electrode at various pH levels. Phenazine methosulfate (PMS) reacted directly at the PQQ domain, whereas cytochrome c (cyt c) reacted via the cytochrome domain of intact CcPDH. Thus, electrons are transferred from reduced PQQ in the catalytic domain of CcPDH to heme b in the N-terminal cytochrome domain, which acts as a built-in mediator and transfers electron to a heterogenous electron transfer protein. The optimal pH values of the PMS reduction (pH 6.5) and the cyt c reduction (pH 8.5) differ. The catalytic currents for the oxidation of L-fucose were observed within a range of pH 4.5 to 11. Bioelectrocatalysis of CcPDH based on direct electron transfer demonstrated that the pH profile of the biocatalytic current was similar to the reduction activity of cyt c characters. - Highlights: • pH dependencies of activity were different for the reduction of cyt c and DCPIP. • DET-based bioelectrocatalysis of CcPDH was observed. • The similar pH-dependent profile was found with cyt c and electrode. • The present results suggested that IET reaction of CcPDH shows pH dependence.},
doi = {10.1016/J.BBRC.2016.06.096},
url = {https://www.osti.gov/biblio/22606167}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 477,
place = {United States},
year = {2016},
month = {8}
}