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dc.contributor.advisorKamer, Paul (Paul C. J.)
dc.contributor.authorDeuss, Peter J.
dc.descriptionElectronic version excludes material for which permission has not been granted by the rights holderen_US
dc.description.abstractThis thesis describes the design, synthesis and application of artificial metalloenzymes for transition metal catalysed reactions not performed by natural enzymes. Unique cysteine containing protein templates were covalently modified with transition metal ligand complexes that generate catalytic activity, which allows for the use of virtually any protein template. SCP-2L was selected as template for the linear hydrophobic tunnel that traverses the protein, which has high affinity for linear aliphatic molecules. The use of catalysts based on this protein to induce increased activity in the biphasic hydroformylation of linear α-olefins is investigated in this work. For this purpose, unique cysteine containing mutants of SCP-2L were modified with phosphine ligands by application of a novel bioconjugation procedure. Application of rhodium adducts of the phosphine modified protein constructs led to up to a 100 fold increase of the turn over numbers was measured compared to a Rh/TPPTS model system which is used in industry. Furthermore, good selectivity towards the linear product was observed. If it can be confirmed that the found catalytic results truly are the result of substrate encapsulation by the protein scaffold, this system represents the first rationally designed artificial metalloenzyme which exploits the shape selectivity of the protein scaffold to direct the outcome of a catalytic reaction. In addition, a study was performed for the development of enantioselective artificial metalloenzymes. Nitrogen ligands were covalently introduced in SCP-2L and the obtained conjugates were applied in the copper catalysed Diels-Alder and Michael addition reaction. A promising 25% ee was found for the Diels-Alder reaction between azachalcone and cyclopentadiene using one of the created constructs. Further development of these catalyst systems with the use of both synthetic (e.g. optimisation of ligand structure) and biomolecular tools (e.g. optimisation of protein environment) for optimisation can lead to very efficient and enantioselective conversions in the future.en_US
dc.publisherUniversity of St Andrews
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported
dc.subjectArtificial metalloenzymesen_US
dc.subjectPhosphine ligandsen_US
dc.subject.lcshProteins--Chemical modificationen_US
dc.subject.lcshTransition metal catalystsen_US
dc.titleArtificial metalloenzymes : modified proteins as tuneable transition metal catalystsen_US
dc.contributor.sponsorSasol Technology UKen_US
dc.type.qualificationnamePhD Doctor of Philosophyen_US
dc.publisher.institutionThe University of St Andrewsen_US
dc.rights.embargoreasonThesis restricted in accordance with University regulations. Print and electronic copy restricted until 22nd November 2017en_US

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Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported
Except where otherwise noted within the work, this item's license for re-use is described as Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported