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Electroanalytical characterization of the direct Marinobacter hydrocarbonoclasticus nitric oxide reductase-catalysed nitric oxide and dioxygen reduction

dc.contributor.authorGomes, Filipa O.
dc.contributor.authorMaia, Luísa B.
dc.contributor.authorCordas, Cristina
dc.contributor.authorMoura, Isabel
dc.contributor.authorDelerue-Matos, Cristina
dc.contributor.authorMoura, José J.G.
dc.contributor.authorMorais, Simone
dc.date.accessioned2020-10-30T14:59:39Z
dc.date.available2020-10-30T14:59:39Z
dc.date.issued2019
dc.description.abstractUnderstanding the direct electron transfer processes between redox proteins and electrode surface is fundamental to understand the proteins mechanistic properties and for development of novel biosensors. In this study, nitric oxide reductase (NOR) extracted from Marinobacter hydrocarbonoclasticus bacteria was adsorbed onto a pyrolytic graphite electrode (PGE) to develop an unmediated enzymatic biosensor (PGE/NOR)) for characterization of NOR direct electrochemical behaviour and NOR electroanalytical features towards NO and O2. Square-wave voltammetry showed the reduction potential of all the four NOR redox centers: 0.095 ± 0.002, -0.108 ± 0.008, -0.328 ± 0.001 and -0.635 ± 0.004 V vs. SCE for heme c, heme b, heme b3 and non-heme FeB, respectively. The determined sensitivity (-4.00 × 10-8 ± 1.84 × 10-9 A/μM and - 2.71 × 10-8 ± 1.44 × 10-9 A/μM for NO and O2, respectively), limit of detection (0.5 μM for NO and 1.0 μM for O2) and the Michaelis Menten constant (2.1 and 7.0 μM for NO and O2, respectively) corroborated the higher affinity of NOR for its natural substrate (NO). No significant interference on sensitivity towards NO was perceived in the presence of O2, while the O2 reduction was markedly and negatively impacted (3.6 times lower sensitivity) by the presence of NO. These results clearly demonstrate the high potential of NOR for the design of innovative NO biosensors.pt_PT
dc.description.sponsorshipFG and LBM thank FCT/MCTES for the fellowship grants SFRH/BD/52502/2014 and SFRH/BPD/111404/2015, respectively, which are financed by national funds and co-financed by FSE. CMC acknowledges FCT-MCTES funding through project PTDC/BBB-BQB/0129/2014 (FCT/MCTES). This work was supported by the REQUIMTE, which is financed by national funds from FCT/MCTES (UID/QUI/50006/2013 and UID/Multi/04378/2013) and co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007265 and POCI-01-0145-FEDER-007728), and also by the PTDC/BB-BQB/0129/2014 project (FCT/MCTES). Funding through REQUIMTE project entitled “NOR-based biosensor for nitric oxide detection in biological and environmental samples” is also acknowledged.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1016/j.bioelechem.2018.08.005pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.22/16395
dc.language.isoengpt_PT
dc.publisherElsevierpt_PT
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S1567539418301609?via%3Dihubpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectBacterial Proteinspt_PT
dc.subjectBiosensing Techniquespt_PT
dc.subjectElectrochemical Techniquespt_PT
dc.subjectElectron Transportpt_PT
dc.subjectHeme proteinspt_PT
dc.subjectLimit of Detectionpt_PT
dc.subjectMarinobacterpt_PT
dc.subjectNitric Oxidept_PT
dc.subjectOxidation-Reductionpt_PT
dc.subjectOxidoreductasespt_PT
dc.subjectOxygenpt_PT
dc.subjectDirect electron transferpt_PT
dc.subjectNitric oxide reductasept_PT
dc.subjectNitric oxide bioelectrocatalysispt_PT
dc.subjectDioxygen bioelectrocatalysispt_PT
dc.titleElectroanalytical characterization of the direct Marinobacter hydrocarbonoclasticus nitric oxide reductase-catalysed nitric oxide and dioxygen reductionpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FQUI%2F50006%2F2013/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04378%2F2013/PT
oaire.citation.endPage14pt_PT
oaire.citation.startPage8pt_PT
oaire.citation.titleBioelectrochemistrypt_PT
oaire.citation.volume125pt_PT
oaire.fundingStream5876
oaire.fundingStream5876
person.familyNameO. Gomes
person.familyNameDelerue-Matos
person.familyNameMorais
person.givenNameFilipa
person.givenNameCristina
person.givenNameSimone
person.identifier1598822
person.identifier.ciencia-id0811-1421-0FD8
person.identifier.ciencia-id9A1A-43FB-5C27
person.identifier.ciencia-idB111-BBFB-F200
person.identifier.orcid0000-0002-9050-4557
person.identifier.orcid0000-0002-3924-776X
person.identifier.orcid0000-0001-6433-5801
person.identifier.ridO-4202-2015
person.identifier.ridD-4990-2013
person.identifier.scopus-author-id6603741848
person.identifier.scopus-author-id7007053747
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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