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The complexes of the fluorescence probe coumarin 153 with apomyoglobin and apoleghemoglobin are used as model systems to study solvation dynamics in proteins. Time- resolved Stokes shift experiments are compared with molecular dynamics simulations, and very good agreement is obtained. Solvation of the coumarin probe is very rapid with approximately 60% occurring within 300 fs and is attributed to interactions with water (or possibly to the protein itself). Differences in the solvation relaxation (or correlation) function, C(t), for the two proteins are attributed to differences in their heme pockets.  Reprinted with permission from Journal of Chemical Physics, 2007, 127 (5), 05501-055106 Copyright (2007) American Institute of Physics. Departments of Chemistry and Biochemistry, Biophysics, and Molecular Biology Iowa State University; Ames, Iowa 50011 USA. * Author to whom all correspondence should be addressed.

Use of steady-state and time-resolved fluorescence spectroscopy as a tool to investigate photophysics of biologically and environmentally relevant systems