Kinetic and thermodynamic analysis of Cu2+-dependent reductive inactivation in direct electron transfer-type bioelectrocatalysis by copper efflux oxidase
dc.rights.license | open | en_US |
dc.contributor.author | ADACHI, Taiki | |
dc.contributor.author | MAZURENKO, Ievgen | |
hal.structure.identifier | Centre de Recherche Paul Pascal [CRPP] | |
dc.contributor.author | MANO, Nicolas | |
dc.contributor.author | KITAZUMI, Yuki | |
dc.contributor.author | KATAOKA, Kunishige | |
dc.contributor.author | KANO, Kenji | |
dc.contributor.author | SOWA, Keisei | |
dc.contributor.author | LOJOU, Elisabeth | |
dc.date.accessioned | 2022-10-29T09:27:01Z | |
dc.date.available | 2022-10-29T09:27:01Z | |
dc.date.issued | 2022-10-01 | |
dc.identifier.issn | 0013-4686 | en_US |
dc.identifier.uri | oai:crossref.org:10.1016/j.electacta.2022.140987 | |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/170152 | |
dc.description.abstractEn | Copper efflux oxidases (CueOs) are key enzymes in copper homeostasis systems. The mechanisms involved are however largely unknown. CueO-type enzymes share a typical structural feature composed of Methionine-rich (Met-rich) domains that are proposed to be involved in copper homeostasis. Bioelectrocatalysis using CueO-type enzymes in the presence of Cu2+ recently highlighted a new Cu2+-dependent catalytic pathway related to a cuprous oxidase activity. In this work, we further investigated the effects of Cu2+ on direct electron transfer (DET)-type bioelectrocatalytic reduction of O2 by CueO at NH2-functionalized multi-walled carbon nanotubes. The DET-type bioelectrocatalytic activity of CueO decreased at low potential in the presence of Cu2+, showing unique peak-shaped voltammograms that we attribute to inactivation and reactivation processes. Chronoamperometry was used to kinetically analyze these processes, and the results suggested linear free energy relationships between the inactivation/reactivation rate constant and the electrode potential. Pseudo-steady-state analysis also indicated that Cu2+ uncompetitively inhibited the enzymatic activity. A detailed model for the Cu2+-dependent reductive inactivation of CueO was proposed to explain the electrochemical data, and the related thermodynamic and kinetic parameters. A CueO variant with truncated copper-binding α helices and bilirubin oxidase free of Met-rich domains also showed such reductive inactivation process, which suggests that multicopper oxidases contain copper-binding sites that lead to inactivation. | |
dc.language.iso | EN | en_US |
dc.source | crossref | |
dc.subject.en | Multicopper oxidase | |
dc.subject.en | Copper efflux oxidase | |
dc.subject.en | Direct electron transfer | |
dc.subject.en | Bioelectrochemistry | |
dc.subject.en | Cu2+ effects | |
dc.title.en | Kinetic and thermodynamic analysis of Cu2+-dependent reductive inactivation in direct electron transfer-type bioelectrocatalysis by copper efflux oxidase | |
dc.type | Article de revue | en_US |
dc.identifier.doi | 10.1016/j.electacta.2022.140987 | en_US |
dc.subject.hal | Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire | en_US |
bordeaux.journal | Electrochimica Acta | en_US |
bordeaux.page | 140987 | en_US |
bordeaux.volume | 429 | en_US |
bordeaux.hal.laboratories | Centre de Recherche Paul Pascal (CRPP) - UMR 5031 | en_US |
bordeaux.institution | Université de Bordeaux | en_US |
bordeaux.institution | CNRS | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
bordeaux.import.source | dissemin | |
hal.export | false | |
workflow.import.source | dissemin | |
dc.rights.cc | Pas de Licence CC | en_US |
bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Electrochimica%20Acta&rft.date=2022-10-01&rft.volume=429&rft.spage=140987&rft.epage=140987&rft.eissn=0013-4686&rft.issn=0013-4686&rft.au=ADACHI,%20Taiki&MAZURENKO,%20Ievgen&MANO,%20Nicolas&KITAZUMI,%20Yuki&KATAOKA,%20Kunishige&rft.genre=article |
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