Spectral hole burning study of protoporphyrin IX substituted myoglobin

J. Zollfrank, J. Friedrich, F. Parak

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Abstract

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.

Original languageEnglish
Pages (from-to)716-724
Number of pages9
JournalBiophysical Journal
Volume61
Issue number3
DOIs
StatePublished - 1992
Externally publishedYes

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