CANCELLED - McCamley Lecture

This lecture has unfortunately now been cancelled due to Covid 19

Abstract:
Genetic code expansion has drastically increased the number of amino acids we can incorporate into protein scaffolds, and includes a number of metal-binding amino acids. Bipyridylalanine is of particular interest to biocatalyst designers as bipyridine is a well-known ligand in coordination chemistry and has been extensively studied by the chemical community in multiple applications over the last 100 years. As a rigid bidentate ligand, it offers different structural binding motifs to the canonical amino acids and the possibility of building up very different metal active sites to enable new-to-nature chemistry to be introduced to metalloenzymes. In this talk I will describe my group’s forays into designing artificial metalloenzymes containing bipyridylalanine, including how we have confirmed the active site structures and their applications in Cu, Ru and Ir catalysis.

About the Jarvis group:
Our research group is interested in the application of biological architecture to the design of transition-metal catalysts, to develop highly selective catalysts for ‘unnatural’ reactions such as hydroformylation, direct C-H functionalisation. We are fascinated by the opportunities that artificial metalloenzymes offer in terms of enhancing selectivity and reactivity of reactions, whilst also offering routes towards more sustainable chemistry. We are interested in obtaining a well-rounded understanding of the catalysts and their reactions, and thus study catalyst development from a number of different perspectives such as enzyme engineering, inorganic/organometallic catalyst development and the application of these catalysis in chemical synthesis

Hosts: Lukas Geciauskas - lg1088@york.ac.uk; Alice Hewson - arh567@york.ac.uk

More information on the McCamley Lecture Series