Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes

Direct electron transfer reactions of high redox potential Trametes hirsuta laccase on bare and 15 different thiol‐modified gold electrodes were studied using cyclic voltammetry and potentiometry. Well‐pronounced Faradaic processes were obtained for the enzyme adsorbed on bare gold, whereas reproduc...

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Autores: Shleev, Sergey, Pita, Marcos, Yaropolov, Alexander I., Ruzgas, Tautgirdas, Gorton, Lo
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2006
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/163612
Acceso en línea:http://hdl.handle.net/10261/163612
Access Level:acceso abierto
Palabra clave:Laccase
T1, T2, and T3 sites
Redox potential
Gold electrode
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spelling Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold ElectrodesShleev, SergeyPita, MarcosYaropolov, Alexander I.Ruzgas, TautgirdasGorton, LoLaccaseT1, T2, and T3 sitesRedox potentialGold electrodeDirect electron transfer reactions of high redox potential Trametes hirsuta laccase on bare and 15 different thiol‐modified gold electrodes were studied using cyclic voltammetry and potentiometry. Well‐pronounced Faradaic processes were obtained for the enzyme adsorbed on bare gold, whereas reproducible and stable electrochemistry was obtained only when 4‐aminothiophenol was used for gold modification. Moreover, the laccase‐4‐aminothiophenol‐modified gold electrode showed the highest value of the steady‐state potential under aerobic conditions equal to 660 mV vs. NHE compared with the other 15 different thiol modified electrodes and also the bare electrodes with immobilized enzyme. However, this value is still too far away from the equilibrium potential of the oxygen electrode and Trametes hirsuta laccase‐modified graphite electrode, for which a well‐pronounced high potential process of oxygen bioelectroreduction is shown at 800 mV vs. NHE. Possible mechanisms of the enzyme function on bare and thiol‐modified gold electrodes are discussed in correlation with the structure and orientation of the enzyme on the surface of the various electrodes.The work was supported by the Swedish Research Council, the Swedish Institute (SI), the Consejería de Educación de la Comunidad de Madrid, and the European Social Funding (F. S. E.). The SI is acknowledged for the support of a postdoctoral fellowship for S. S.Peer reviewedJohn Wiley & SonsSwedish Research CouncilSwedish InstituteComunidad de MadridEuropean CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201820182006info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/163612reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1002/elan.200603600Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1636122026-05-22T06:33:51Z
dc.title.none.fl_str_mv Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
title Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
spellingShingle Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
Shleev, Sergey
Laccase
T1, T2, and T3 sites
Redox potential
Gold electrode
title_short Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
title_full Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
title_fullStr Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
title_full_unstemmed Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
title_sort Direct Heterogeneous Electron Transfer Reactions of Trametes hirsuta Laccase at Bare and Thiol‐Modified Gold Electrodes
dc.creator.none.fl_str_mv Shleev, Sergey
Pita, Marcos
Yaropolov, Alexander I.
Ruzgas, Tautgirdas
Gorton, Lo
author Shleev, Sergey
author_facet Shleev, Sergey
Pita, Marcos
Yaropolov, Alexander I.
Ruzgas, Tautgirdas
Gorton, Lo
author_role author
author2 Pita, Marcos
Yaropolov, Alexander I.
Ruzgas, Tautgirdas
Gorton, Lo
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Swedish Research Council
Swedish Institute
Comunidad de Madrid
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Laccase
T1, T2, and T3 sites
Redox potential
Gold electrode
topic Laccase
T1, T2, and T3 sites
Redox potential
Gold electrode
description Direct electron transfer reactions of high redox potential Trametes hirsuta laccase on bare and 15 different thiol‐modified gold electrodes were studied using cyclic voltammetry and potentiometry. Well‐pronounced Faradaic processes were obtained for the enzyme adsorbed on bare gold, whereas reproducible and stable electrochemistry was obtained only when 4‐aminothiophenol was used for gold modification. Moreover, the laccase‐4‐aminothiophenol‐modified gold electrode showed the highest value of the steady‐state potential under aerobic conditions equal to 660 mV vs. NHE compared with the other 15 different thiol modified electrodes and also the bare electrodes with immobilized enzyme. However, this value is still too far away from the equilibrium potential of the oxygen electrode and Trametes hirsuta laccase‐modified graphite electrode, for which a well‐pronounced high potential process of oxygen bioelectroreduction is shown at 800 mV vs. NHE. Possible mechanisms of the enzyme function on bare and thiol‐modified gold electrodes are discussed in correlation with the structure and orientation of the enzyme on the surface of the various electrodes.
publishDate 2006
dc.date.none.fl_str_mv 2006
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/163612
url http://hdl.handle.net/10261/163612
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1002/elan.200603600
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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