Publication | Closed Access
Activation Energy Spectrum of a Biomolecule: Photodissociation of Carbonmonoxy Myoglobin at Low Temperatures
130
Citations
5
References
1974
Year
EngineeringCarbonmonoxy MyoglobinOptical PropertiesPhotophysical PropertyMolecular SpectroscopyBiophysicsEnergy SpectrumBiochemistryPhotochemistryPhysicsMechanistic PhotochemistryActivation Energy SpectrumPhysical ChemistryLow TemperaturesNatural SciencesSpectroscopyCarbon Monoxide BoundActivation-energy SpectrumQuantum Biology
Carbon monoxide bound to myoglobin can be photodissociated with high quantum yield. The subsequent rebinding can be followed optically. In the temperature range between 40 and 200 K, rebinding can be described by a function of the form ${t}_{0}$, where $n$ and $H(t)={(1+\frac{t}{{t}_{0}})}^{\ensuremath{-}n}$ are temperature-dependent parameters. This behavior can be explained by assuming the existence of an activation-energy spectrum; the form of this spectrum is determined. The energy spectrum may be due to the existence of myoglobin conformers.
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