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dc.contributor.authorGoetze, Jan Philipp
dc.contributor.authorBuehl, Michael
dc.date.accessioned2017-08-17T23:33:02Z
dc.date.available2017-08-17T23:33:02Z
dc.date.issued2016-09-08
dc.identifier.citationGoetze , J P & Buehl , M 2016 , ' Laccase redox potentials: pH dependence and mutants, a QM/MM study ' , Journal of Physical Chemistry B , vol. 120 , no. 35 , pp. 9265-9276 . https://doi.org/10.1021/acs.jpcb.6b04978en
dc.identifier.issn1520-6106
dc.identifier.otherPURE: 245112100
dc.identifier.otherPURE UUID: 49bb75f3-d5fb-4bd8-9702-0c94fd5f49d0
dc.identifier.otherScopus: 84986270048
dc.identifier.otherORCID: /0000-0002-1095-7143/work/48131778
dc.identifier.otherWOS: 000383005200001
dc.identifier.urihttps://hdl.handle.net/10023/11500
dc.descriptionThe authors are grateful for funding by the Engineering and Physical Sciences Research Council, grant “Clean catalysis for sustainable development” (Ref. EP/J018139/1).en
dc.description.abstractWe have studied the T. versicolor laccase T1 site redox potential (RP) at the M06/6-311++G**/SDD(Cu) level of theory, employing QM/MM optimised geometries (RI-BP86/def2-SVP/def2-TZVP(Cu):CHARMM) of the whole protein system with electronic embedding. The oxidation state of the trinuclear cluster was found to affect the T1 site RP by about 0.2-0.3 V, depending on the protein protonation state. The computed laccase RP can be drastically lowered upon introduction of a protonation state corresponding to a neutral environment, by up to -1.37 V, which is likely an overestimation of the effect in vivo. The gradual change of the protonation state by single points without optimisation or equilibration results in a change that is even larger, namely up to about -2.6 V. Thus, the preferred protein conformation supports a high redox potential, compensating for the RP-lowering effect of surface charges. The predicted change in RP on going to the F463M mutant, ca. -0.1 V, is consistent with observations for a related laccase. Based on our results, we also propose and test a D206N mutant, but find it to be locked in a conformation with slightly lower RP.
dc.format.extent12
dc.language.isoeng
dc.relation.ispartofJournal of Physical Chemistry Ben
dc.rightsCopyright © 2016 American Chemical Society. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://dx.doi.org/10.1021/acs.jpcb.6b04978en
dc.subjectQD Chemistryen
dc.subjectDASen
dc.subject.lccQDen
dc.titleLaccase redox potentials: pH dependence and mutants, a QM/MM studyen
dc.typeJournal articleen
dc.contributor.sponsorEPSRCen
dc.description.versionPostprinten
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1021/acs.jpcb.6b04978
dc.description.statusPeer revieweden
dc.date.embargoedUntil2017-08-17
dc.identifier.grantnumberEP/J018139/1en


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