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dc.contributor.authorCastro, Ludovic
dc.contributor.authorCrawford, Luke
dc.contributor.authorMutengwa, Archford
dc.contributor.authorGoetze, Jan Philipp
dc.contributor.authorBuehl, Michael
dc.date.accessioned2016-03-23T15:00:07Z
dc.date.available2016-03-23T15:00:07Z
dc.date.issued2016-02-28
dc.identifier240256977
dc.identifierc878f630-4c76-4ab8-b27e-98ea9be9feca
dc.identifier84983110931
dc.identifier000370877700002
dc.identifier.citationCastro , L , Crawford , L , Mutengwa , A , Goetze , J P & Buehl , M 2016 , ' Insights into structure and redox potential of lignin peroxidase from QM/MM calculations ' , Organic & Biomolecular Chemistry , vol. 14 , no. 8 , pp. 2385-2389 . https://doi.org/10.1039/C6OB00037Aen
dc.identifier.issn1477-0520
dc.identifier.otherORCID: /0000-0002-1095-7143/work/48131767
dc.identifier.urihttps://hdl.handle.net/10023/8473
dc.descriptionThe authors wish to thank EaStCHEM, the School of Chemistry and the EPSRC (grant code EP/J018139/1) for fundingen
dc.description.abstractRedox potentials are computed for the active form (compound I) of lignin peroxidase (LiP) using a suitable QM/MM methodology (B3LYP/SDD/6-311G**//BP86/SVP:CHARMM). Allowing for dynamic conformational averaging, a potential of 0.67(33) V relative to ferrocenium/ferrocene is obtained for the active form with its oxoiron(IV) core. The computed redox potential is very sensitive to the charge distribution around the active site: protonation of titratable residues close to the metal center increases the redox potential, thereby rationalising the known pH dependence of LiP activity. A simple MM-charge deletion scheme is used to identify residues that are critical for the redox potential. Two mutant proteins are studied through homology modelling, E40Q and D183N, which are predicted to have an increased redox potential by 140 mV and 190 mV, respectively, relative to the wild type. These mutant proteins are thus promising targets for synthesis and further exploration toward a rational design of biocatalytic systems for oxidative degradation of lignin.
dc.format.extent787560
dc.language.isoeng
dc.relation.ispartofOrganic & Biomolecular Chemistryen
dc.subjectQD Chemistryen
dc.subjectDASen
dc.subject.lccQDen
dc.titleInsights into structure and redox potential of lignin peroxidase from QM/MM calculationsen
dc.typeJournal articleen
dc.contributor.sponsorEPSRCen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doi10.1039/C6OB00037A
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.rsc.org/suppdata/c6/ob/c6ob00037a/c6ob00037a1.pdfen
dc.identifier.grantnumberEP/J018139/1en


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