Solvation dynamics in protein environments: Comparison of fluorescence upconversion measurements of coumarin 153 in monomeric hemeproteins with molecular dynamics simulations

Mintu Halder, Prasun Mukherjee, Sayantan Bose, Mark S. Hargrove, Xueyu Song, Jacob W. Petrich
2007 Journal of Chemical Physics  
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. The solvation of the coumarin probe is very rapid with approximately 60% occurring within 300fs and is attributed to interactions with water (or possibly to the protein itself). Differences in the solvation
more » ... n (or correlation) function C(t) for the two proteins are attributed to differences in their hemepockets.
doi:10.1063/1.2753495 pmid:17688362 fatcat:hcsooshyejesla4sfm63umxyoq