Abstract
The unidirectional circulation of an enzyme round a working cycle can be understood in terms of the formation and decay of a soliton that acts as a ligand for the protein and for which the surrounding heat bath serves as a sink. An experimental confirmation of this interpretation is suggested in which the soliton is of the Davidov type and is created by infrared photon absorption as in recent experiments on acetanilide.
Keywords: enzyme, nonequilibrium, kinetic linkage, free energy transduction
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Selected References
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