Volume 97, Number 2, January 2012
|Number of page(s)||6|
|Published online||18 January 2012|
A solution to the subdiffusion-efficiency paradox: Inactive states enhance reaction efficiency at subdiffusion conditions in living cells
Department of Physics, Technical University of Munich - James-Franck Straße, D-85747 Garching, Germany, EU
2 MEMPHYS - Center for Biomembrane Physics, Department of Physics, Chemistry and Pharmacy, University of Southern Denmark - Campusvej 55, DK-5230 Odense M, Denmark, EU
3 Institute for Physics and Astronomy, University of Potsdam - D-14476 Potsdam-Golm, Germany, EU
4 Department of Physics, Tampere University of Technology - FI-33101 Tampere, Finland, EU
Accepted: 12 December 2011
Macromolecular crowding in living biological cells effects subdiffusion of larger biomolecules such as proteins and enzymes. Mimicking this subdiffusion in terms of random walks on a critical percolation cluster, we here present a case study of EcoRV restriction enzymes involved in vital cellular defence. We show that due to its so far elusive propensity to an inactive state the enzyme avoids non-specific binding and remains well-distributed in the bulk cytoplasm of the cell. Despite the reduced volume exploration capability of subdiffusion processes, this mechanism guarantees a high efficiency of the enzyme. By variation of the non-specific binding constant and the bond occupation probability on the percolation network, we demonstrate that reduced non-specific binding are beneficial for efficient subdiffusive enzyme activity even in relatively small bacteria cells. Our results corroborate a more local picture of cellular regulation.
PACS: 05.40.-a – Fluctuation phenomena, random processes, noise, and Brownian motion / 87.10.-e – General theory and mathematical aspects / 87.16.-b – Subcellular structure and processes
© EPLA, 2012
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