Abstract
The kinetics of ligand binding to heme proteins studied by flash photolysis display an algebraic time dependence at low temperatures in contrast exponential recombination observed under physiological conditions. This result shows that protein structures should be viewed as a time average of interconverting microstates which are frozen in at low temperatures. We propose a quasi-one-dimensional model of heterogeneous structural diffusion coupled to ligand binding which describes freezing transition as an inherent property of protein fluctuations. The structural hopping rates are derived from a temperature invariant spectrum of activation energies. The model predicts power law kinetics of the form t -β at long times. The exponent β is constant (0.5) at high temperatures but decreases below a critical temperature in the frozen regime. These results are compared to experiments performed with myoglobin and β-chains of hemoglobin.
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Doster, W., Holzhey, C., Miesmer, H. et al. The effect of heterogeneous structural diffusion on ligand binding to heme proteins. J Biol Phys 17, 281–295 (1990). https://doi.org/10.1007/BF00386603
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DOI: https://doi.org/10.1007/BF00386603