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BP: Fachverband Biologische Physik
BP 26: Focus Session: Bioinspired Systems
BP 26.5: Vortrag
Donnerstag, 8. September 2022, 16:30–16:45, H15
Synchronization, enhanced catalysis of mechanically coupled enzymes and how to design them — •Michalis Chatzittofi1, Jaime Agudo-Canalejo1, Tunrayo Adeleke-Larodo2, Pierre Illien3, and Ramin Golestanian1,2 — 1Department of Living Matter Physics, MPI -DS, D-37077 Göttingen, Germany — 2Rudolf Peierls Centre for Theoretical Physics, University of Oxford, OX1 3PU, UK — 3Sorbonne Universite, CNRS, Laboratoire Physicochimie des Electrolytes et Nanosystemes Interfaciaux, 75005, France
Enzymes are the catalysts of the chemical processes that take place in living organisms. These processes, during which chemical energy is converted to mechanical energy and heat, occur stochastically as a result of a noise-activated barrier-crossing event. Despite this stochasticity, it has been shown recently that two mechanically coupled enzymes can synchronize their catalytic reaction [1]. Even more interestingly, the coupling enhances the catalysis of the two enzymes. This effect can be understood as arising from a bifurcation in the deterministic dynamics of the system. In this work, we use a similar approach to describe the dynamics of an enzyme by assuming that the enzyme is attached to a passive molecule. The goal is to design the properties of the enzyme so that its motion favours a chemical reaction, for example dissociation or a shape switch of the molecule. A bifurcation in the deterministic dynamics can cause a change in the molecules state after one enzymatic reaction. The stochastic simulations, also show that the enzyme's activity affects the state of the molecule.
[1] J. Agudo-Canalejo, et al., Phys. Rev. Lett. 127, 208103 (2021).