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Artificial metalloenzyme design with late transition metal active sites


Project Description

This PhD project involves the rational design, preparation and assessment of artificial metalloenzymes. Nature’s catalysts, enzymes, have been perfected by evolution to perform reactions under mild conditions and with enviable asymmetric control and selectivity. However, the active sites of metalloenzymes are primarily restricted to first row transition metals, despite catalysis with heavier transition metals offering more diversity in terms of reactivity. This is primarily due to these heavier metals not being “biologically available”. This PhD project will combine the advantages afforded by both the xenobiotic and the enzymatic catalytic worlds, so as to create new biotechnology for the efficient and catalytic synthesis of complex molecules.

Xenobiotic catalytic sites will be engineered into increasingly complex and structured peptide and protein assemblies. This includes, but is not limited to de novo designed miniature artificial protein scaffolds, specifically coiled coils (see Figure). The resulting artificial metalloenzymes with xenobiotic active sites will be screened for asymmetric catalysis, and used to establish key structure-function relationships. This is a multidisciplinary project incorporating elements of asymmetric chemical catalysis and synthetic biology.

This studentship is competition funded by the BBSRC MIBTP scheme: http://www.birmingham.ac.uk/research/activity/mibtp/index.aspx

Please contact Dr Anna Peacock () or Dr Paul Davies () directly for more information.

Deadline: 15 December 2019

Expected Stipend: £ 15,200 per annum (plus travel allowance in year one and a MacBook Pro)

The Midlands Integrative Biosciences Training Partnership (MIBTP) is a BBSRC-funded doctoral training partnership between the universities of Warwick, Birmingham and Leicester. It delivers innovative, world-class research training across the Life Sciences to boost the growing Bioeconomy across the UK.

To check your eligibility to apply for this project please visit: http://www2.warwick.ac.uk/fac/cross_fac/mibtp/pgstudy/phd_opportunities/application/

Funding Notes

This studentship is competition funded by the BBSRC MIBTP scheme: View Website

Expected Stipend: £ 15,200 per annum (plus travel allowance in year one and a MacBook Pro)

The Midlands Integrative Biosciences Training Partnership (MIBTP) is a BBSRC-funded doctoral training partnership between the universities of Warwick, Birmingham and Leicester. It delivers innovative, world-class research training across the Life Sciences to boost the growing Bioeconomy across the UK.

To check your eligibility to apply for this project please visit: View Website

References

[1] Peacock, A. F. A.; Bullen, G. A.; Gethings, L.; Williams, J. P.; Kriel, F. H.; Coates, J. “Gold-Phosphine Binding to De Novo Designed Coiled Coil Peptides”, J. Inorg. Biochem., 2012, 117, 298.
[2] Adcock, H. V.; Chatzopoulou, E.; Davies, P. W. “Divergent C-H Insertion-Cyclization Cascades of N-Allyl Ynamides” Angew. Chem. Int. Ed. 2015, 54, 15525.
[3] Berwick, M. R.; Lewis, D. J.; Pikramenou, Z.; Jones, A. W.; Cooper, H. J.; Wilkie, J.; Britton, M. M.; Peacock, A. F. A. “De Novo Design of Ln(III) Coiled Coils for Imaging Applications” J. Am. Chem. Soc., 2014, 136, 1166.
[4] Zastrow, M.; Peacock, A. F. A.; Stuckey, J.; Pecoraro, V. L. “Hydrolytic Catalysis and Structural Stabilization in a Designed Metalloprotein” Nature Chem., 2012, 4, 118.
[5] Ball, Z. T., “Designing Enzyme-like Catalysts: A Rhodium(II) Metallopeptide Case Study” Acc. Chem. Res., 2013, 46, 560.

How good is research at University of Birmingham in Chemistry?

FTE Category A staff submitted: 28.00

Research output data provided by the Research Excellence Framework (REF)

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