Chemical catalysis is used to take cheap, raw chemical feedstocks and convert them efficiently into complex, high value, chemicals. During the outgoing phase of my Marie-Curie Fellowship I work on the development of novel artificial metalloenzymes for chemical catalysis. Artificial metalloenzymes consists of a transition metal embedded in a protein scaffold host. Here the transition metal controls the core reactivity of the catalyst and the surrounding protein host can influence aspects of the reaction such as rate and selectivity. We believe that an optimised artificial metalloenzyme can be used to generate chemicals that have been previously inaccessible by conventional transition metal catalysis. This is a relatively new area of catalysis and only a small number of proteins have been used to host transition metals to create metalloenzymes. Our first objective is to create a metalloenzymes based on novel protein host that displays unique and improved properties over previously developed artificial metalloenzymes. Our second objective is focused on the development of a technology for the optimisation of metalloenzyme catalyst. The proteins that are used to host transition metals are often difficult to synthesis, and with the application of genetic techniques, as many different mutants of each protein are available (>1 million). Making 1 million different proteins to use as metalloenzymes is not practical. We are developing technology for the high-throughput synthesis and reaction screening of a library of metalloenzymes. This technology will hopefully allow for the identification of very active artificial metalloenzymes.