Multiply excited vibration of carbon monoxide in the primary docking site of hemoglobin following photolysis from the heme

Abstract : We investigate ultrafast vibrational ligand dynamics in carboxyhemoglobin using chirped pulse upconversion and demonstrate the formation of vibrationally multiply excited carbon monoxide trapped in the primary docking site of hemoglobin after photolysis. The bleach signal due to ligand dissociation and the incipient docking-site absorption signal are about 200 cm-1 apart and differ by more than an order of magnitude in absorbance. In conventional approaches, these signals are monitored individually. Our method allows simultaneous observation of these signals with both high spectral resolution and high sensitivity. The large amount of vibrationally hot CO in the docking site as observed under Soret band excitation of the heme is discussed in the context of excess energy provided by the pump photon and is shown to be in quantitative agreement with predictions based on changes in the CO equilibrium distance upon instantaneous dissociation. Cop 2010 American Chemical Society.
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Patrick Nuernberger, Kevin Lee, Adeline Bonvalet, Marten Vos, Manuel Joffre. Multiply excited vibration of carbon monoxide in the primary docking site of hemoglobin following photolysis from the heme. Journal of Physical Chemistry Letters, American Chemical Society, 2010, 1 (14), pp.2077. ⟨10.1021/jz1006324⟩. ⟨hal-00805073⟩

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