Findsen E W, Friedman J M, Ondrias M R
Department of Chemistry, University of New Mexico, Albuquerque 87131.
Biochemistry. 1988 Nov 29;27(24):8719-24. doi: 10.1021/bi00424a005.
The heme-pocket dynamics subsequent to carbon monoxide photolysis from human hemoglobin have been monitored as a function of glycerol-water solvent composition with time-resolved resonance Raman spectroscopy. Prompt (geminate) ligand recombination rates and the transient heme-pocket geometry established within 10 ns after photolysis appear to be largely independent of solvent composition. The rate of relaxation of the transient geometry to an equilibrium deoxy configuration is, however, quite sensitive to solvent composition. These observations suggest that the former processes result from local, internal motions of the protein, while the relaxation dynamics of the proximal heme pocket are predicated upon more global protein motions that are dependent upon solvent viscosity.
