Abstract
From the low temperature rebinding kinetics of heme proteins we conclude that a single coordinate description of the biophysical process is insufficient. An additional “protein coordinate” is introduced, which is frozen at low temperatures, and relaxes following dissociation at high temperatures. This relaxation causes the barrier to rebinding to increase with time, leading to a biologically significant “self-cooperativity” effect, on the tertiary-structure level, for a single heme subunit. The predicted effect is supported by recent transient Raman scattering experiments. A second conclusion is that the binding rate coefficient must depend on a fractional power of solvent viscosity. The same non-Kramers behavior has recently been observed also in photochemical isomerization. It may therefore be due to the multi-dimensionality of macromolecular dynamics.
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Agmon, N. (1986). What can be Learned from Low Temperature Reactivity on Room Temperature Rebinding Kinetics of Heme Proteins?. In: Jortner, J., Pullman, B. (eds) Tunneling. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 19. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4752-8_30
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DOI: https://doi.org/10.1007/978-94-009-4752-8_30
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