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Meet the Scientist
My name is Martina Ribar Hestericová (science_exercises.eu on Instagram), and I have recently obtained my PhD. in chemistry aimed at the development and optimization of artificial metalloenzymes. Since then, I have transitioned to industry and become a forensic analytical chemist. I am also an active science communicator and a science journalist, you can read my articles on Chemistry World and on Medium.
The picture shows artificial metalloenzymes. These are created by incorporation of a metal containing cofactor into a host bioscaffold. Our protein of choice is streptavidin, represented in this picture as a sushi ball containing four different types of fish. Each fish represents a monomeric unit, together forming a homotetrameric protein.
Streptavidin has a very high affinity towards biotin, also known as vitamin H. We use this affinity as an anchoring strategy, meaning that we bind the biotin moiety together with the metal catalyst- the resulting biotinylated catalyst is shown here as a pancake.
When we combine this 'catalytic pancake' with the protein, they stuck together thanks to the high Sav-biot affinity.
The resulting hybrid catalyst, aka artificial metalloenzyme, now has a catalytic centre inside of the protein active site (represented by the caviar dots on the sushi ball) and can catalyze even new-to-nature reactions.
 Mallin, H., Hestericová, M., Reuter, R., & Ward, T. R. (2016). Library design and screening protocol for artificial metalloenzymes based on the biotin-streptavidin technology. nature protocols, 11(5), 835.
 Hestericová, M., Heinisch, T., Alonso‐Cotchico, L., Maréchal, J. D., Vidossich, P., & Ward, T. R. (2018). Directed Evolution of an Artificial Imine Reductase. Angewandte Chemie, 130(7), 1881-1886.
 Hestericová, M., Correro, M. R., Lenz, M., Corvini, P. F. X., Shahgaldian, P., & Ward, T. R. (2016). Immobilization of an artificial imine reductase within silica nanoparticles improves its performance. Chemical Communications, 52(60), 9462-9465.
 Hestericová, M. (2018). Directed Evolution of Artificial Metalloenzymes: Genetic Optimization of the Catalytic Activity. CHIMIA International Journal for Chemistry, 72(4), 189-192.
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