Abstract
The ligand binding processes of hemoglobin and myoglobin are among the most extensively studied kinetic mechanisms in biology. In recent years, the photodeligation mechanisms of hemoglobin and myoglobin have been investigated by a number of groups using picosecond absorption spectroscopy [1–4]. In this paper, we present some of our recent results, using a newly developed technique, picosecond time-resolved resonance Raman spectroscopy [5–7], which produces vibrational spectra of transient rather than stable molecules. Flash photolysis techniques, such as picosecond absorption spectroscopy, have been powerful methods for identifying chemical intermediates and providing kinetic rate information. The broad absorptions though, contain only limited structural information. Resonance Raman spectroscopy, on the other hand, is capable of providing detailed vibrational information [8] and can be time-resolved using pulsed laser techniques [9].
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Terner, J., Spiro, T.G., Voss, D.F., Paddock, C., Miles, R.B. (1982). Picosecond Time-Resolved Resonance Raman Spectroscopy of the Photolysis Product of Oxy-Hemoglobin. In: Eisenthal, K.B., Hochstrasser, R.M., Kaiser, W., Laubereau, A. (eds) Picosecond Phenomena III. Springer Series in Chemical Physics, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87864-0_79
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DOI: https://doi.org/10.1007/978-3-642-87864-0_79
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