Activation Energy Spectrum of a Biomolecule: Photodissociation of Carbonmonoxy Myoglobin at Low Temperatures
- 25 February 1974
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 32 (8) , 403-405
- https://doi.org/10.1103/physrevlett.32.403
Abstract
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 , where and 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.
Keywords
This publication has 5 references indexed in Scilit:
- Dynamics of Carbon Monoxide Binding by Heme ProteinsScience, 1973
- Protein Structure and FunctionAnnual Review of Physical Chemistry, 1972
- Protein conformation: Autoplastic and alloplastic effectsArchives of Biochemistry and Biophysics, 1966
- Large Temperature Range AnnealingJournal of Applied Physics, 1960
- Kinetics of Processes Distributed in Activation EnergyPhysical Review B, 1955