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

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DOIResolve DOI: https://doi.org/10.1021/jz1006324
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FormatText, Article
Subjectultrafast pump−probe spectroscopy; vibrational spectroscopy; heme proteins; hemoglobin; ligand dissociation; docking site
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.
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  • The Journal of Physical Chemistry Letters 1, no. 14 (21 June 2010): 2077–2081.
LanguageEnglish
Peer reviewedYes
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This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

NPARC number21276806
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Record identifier9496b851-55ef-46d0-9e0d-658917e538ef
Record created2015-10-20
Record modified2020-06-02
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