Spectral hole burning study of protoporphyrin IX substituted myoglobin.
Protoporphyrin IX substituted myoglobin reveals excellent hole burning properties. We investigated the frequency shift of persistent spectral holes under isotropic pressure conditions in a range from 0 to 2.4 MPa. In this range, the protein behaves like an elastic solid. The shift of the holes under pressure shows a remarkable frequency dependence from which the compressibility of the protein can be determined. The compressibility, in turn, allows for an estimation of the equilibrium volume fluctuations. Within the frame of the model used to interpret the pressure data, it is possible to determine the absorption frequency of the isolated chromophore and the associated solvent shift in the protein environment.
Zollfrank
J
J
Institut für Physikalische Chemie, Johannes Gutenberg-Universität, Mainz, Germany.
Friedrich
J
J
Parak
F
F
D000818:Animals; D006736:Horses; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D010777:Photochemistry; D011487:Protein Conformation; D011524:Protoporphyrins / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence
D009211:Myoglobin; D011524:Protoporphyrins; C028025:protoporphyrin IX