Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators

The oxygen reduction efficiency of a laccase-modified electrode was found to depend on the chirality of the oligopeptide linker used to bind the enzyme to the surface. At the same time, the electron transfer between the cathode electrode and the enzyme is improved by using a copper(II) complex with...

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Main Authors:	Kumpei Kashiwagi, Francesco Tassinari, Tomoyuki Haraguchi, Koyel Banerjee-Gosh, Takashiro Akitsu, Ron Naaman
Format:	Article
Language:	English
Published:	MDPI AG 2020-05-01
Series:	Symmetry
Subjects:	chirality oligopeptide laccase copper complex electron transfer
Online Access:	https://www.mdpi.com/2073-8994/12/5/808

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spelling	doaj-f2cf1d070f234716bbd6a146c6dc13c52020-11-25T02:55:17ZengMDPI AGSymmetry2073-89942020-05-011280880810.3390/sym12050808Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper MediatorsKumpei Kashiwagi0Francesco Tassinari1Tomoyuki Haraguchi2Koyel Banerjee-Gosh3Takashiro Akitsu4Ron Naaman5Department of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, JapanDepartment of Chemical and Biological Physics, Weizmann Institute of Science, 234 Herzl Street, Rehovot 76100, IsraelDepartment of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, JapanDepartment of Chemical and Biological Physics, Weizmann Institute of Science, 234 Herzl Street, Rehovot 76100, IsraelDepartment of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, JapanDepartment of Chemical and Biological Physics, Weizmann Institute of Science, 234 Herzl Street, Rehovot 76100, IsraelThe oxygen reduction efficiency of a laccase-modified electrode was found to depend on the chirality of the oligopeptide linker used to bind the enzyme to the surface. At the same time, the electron transfer between the cathode electrode and the enzyme is improved by using a copper(II) complex with amino-acid derivative Schiff base ligand with/without azobenzene moiety as a mediator. The increased electrochemical current under both O<sub>2</sub> and N<sub>2</sub> proves that both the mediators are active towards the enzyme.https://www.mdpi.com/2073-8994/12/5/808chiralityoligopeptidelaccasecopper complexelectron transfer
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Kumpei Kashiwagi Francesco Tassinari Tomoyuki Haraguchi Koyel Banerjee-Gosh Takashiro Akitsu Ron Naaman
spellingShingle	Kumpei Kashiwagi Francesco Tassinari Tomoyuki Haraguchi Koyel Banerjee-Gosh Takashiro Akitsu Ron Naaman Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators Symmetry chirality oligopeptide laccase copper complex electron transfer
author_facet	Kumpei Kashiwagi Francesco Tassinari Tomoyuki Haraguchi Koyel Banerjee-Gosh Takashiro Akitsu Ron Naaman
author_sort	Kumpei Kashiwagi
title	Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators
title_short	Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators
title_full	Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators
title_fullStr	Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators
title_full_unstemmed	Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators
title_sort	electron transfer via helical oligopeptide to laccase including chiral schiff base copper mediators
publisher	MDPI AG
series	Symmetry
issn	2073-8994
publishDate	2020-05-01
description	The oxygen reduction efficiency of a laccase-modified electrode was found to depend on the chirality of the oligopeptide linker used to bind the enzyme to the surface. At the same time, the electron transfer between the cathode electrode and the enzyme is improved by using a copper(II) complex with amino-acid derivative Schiff base ligand with/without azobenzene moiety as a mediator. The increased electrochemical current under both O<sub>2</sub> and N<sub>2</sub> proves that both the mediators are active towards the enzyme.
topic	chirality oligopeptide laccase copper complex electron transfer
url	https://www.mdpi.com/2073-8994/12/5/808
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Electron Transfer via Helical Oligopeptide to Laccase Including Chiral Schiff Base Copper Mediators

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