Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism

Thibault Dartigalongue (1) , François Hache (1)

1 LOB - Laboratoire d'optique et biosciences

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. 2005 Elsevier B.V. All rights reserved

Thibault Dartigalongue, François Hache. Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism. Chemical Physics Letters, 2005, 415 (4-6), pp.313-316. ⟨10.1016/j.cplett.2005.09.022⟩. ⟨hal-00097202⟩