Abstract
Interconversion dynamics of ligand in the primary docking site of myoglobin and hemoglobin in various solvents at 283K was investigated by probing time-resolved vibrational spectra of CO photodissociated from these proteins. The interconversion dynamics in various environments (large viscosity change, solvent imposing constraint effect) are similar to those in aqueous solution, indicating that it is minimally coupled to the solvent-coupled large-scale protein motion.
© 2006 Optical Society of America
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