Long-lived states induced by extended illumination of carbonmonoxy-myoglobin
Myoglobin is a heme-protein that binds small ligands, such as O$\sb2$ and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures ($>$160K) the kinetics of recombination of photodissociated carbonmonoxy-myoglobin are non-exponential, having amplitude components that extend over many orders of magnitude in time. The bound and unbound states of the system have different spectroscopic signatures and the kinetics of recombination can be measured by monitoring the time dependence of the absorption spectrum of the sample after photodissociation.
University of Illinois - Urbana-Champaign
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University of Illinois at Urbana-Champaign