Abstract
A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100 ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one.
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