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dc.contributor.authorJarvis, Amanda
dc.contributor.authorObrecht, Lorenz
dc.contributor.authorDeuss, Peter
dc.contributor.authorLaan, Wouter
dc.contributor.authorGibson, Emma K.
dc.contributor.authorWells, Peter P.
dc.contributor.authorKamer, Paul C J
dc.date.accessioned2017-10-09T15:30:12Z
dc.date.available2017-10-09T15:30:12Z
dc.date.issued2017-10-23
dc.identifier.citationJarvis , A , Obrecht , L , Deuss , P , Laan , W , Gibson , E K , Wells , P P & Kamer , P C J 2017 , ' Enzyme activity by design : an artificial rhodium hydroformylase for linear aldehydes ' , Angewandte Chemie , vol. 129 , no. 44 , pp. 13784-13788 . https://doi.org/10.1002/ange.201705753en
dc.identifier.issn0044-8249
dc.identifier.otherPURE: 250874289
dc.identifier.otherPURE UUID: ad037756-dba6-4e29-b399-311316bfb3e7
dc.identifier.otherScopus: 85029357065
dc.identifier.otherWOS: 000413314800005
dc.identifier.urihttp://hdl.handle.net/10023/11820
dc.descriptionFunding: Marie Curie Individual Fellowship project ArtOxiZymes to AGJ (contract no. H2020-MSCA-IF-2014-657755), EPSRC Critical mass grant ‘Clean catalysis for sustainable development’ (EP/J018139/1) and Sasol (CASE studentship to P.J.D.), EPSRC (EP/K014854/1).en
dc.description.abstractArtificial metalloenzymes (ArMs) are hybrid catalysts that offer a unique opportunity to combine the superior performance of natural protein structures with the unnatural reactivity of transition-metal catalytic centers. Therefore, they provide the prospect of highly selective and active catalytic chemical conversions for which natural enzymes are unavailable. Herein, we show how by rationally combining robust site-specific phosphine bioconjugation methods and a lipid-binding protein (SCP-2L), an artificial rhodium hydroformylase was developed that displays remarkable activities and selectivities for the biphasic production of long-chain linear aldehydes under benign aqueous conditions. Overall, this study demonstrates that judiciously chosen protein-binding scaffolds can be adapted to obtain metalloenzymes that provide the reactivity of the introduced metal center combined with specifically intended product selectivity.
dc.language.isoeng
dc.relation.ispartofAngewandte Chemieen
dc.rights© 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.en
dc.subjectArtificial metalloenzymesen
dc.subjectCatalyst designen
dc.subjectHydroformylationen
dc.subjectPhosphinesen
dc.subjectRhodiumen
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectNDASen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.titleEnzyme activity by design : an artificial rhodium hydroformylase for linear aldehydesen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1002/ange.201705753
dc.description.statusPeer revieweden
dc.identifier.urlhttp://onlinelibrary.wiley.com/doi/10.1002/ange.201705753/full#footer-support-infoen


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