0000000000053494
AUTHOR
J. Zollfrank
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 p…
Thermal irreversibility in optically labeled low-temperature glasses.
We present an investigation of irreversible features of thermal broadening of persistent spectral holes. The investigation is based on temperature-cycling hole-burning experiments performed with a variety of organic glasses doped with rather different probe molecules. The results show a rich temperature dependence. They can, however, be interpreted in terms of the well-known spectral diffusion models, in which we introduced a freezing condition to account for thermal irreversiblity. There is a tunneling regime for low temperatures and an activated regime for high temperatures. In the tunneling regime the broadening is linear in T; in the activated regime it increases with ${T}^{3/2}$ and lo…
Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase
For the first time, conformational relaxation processes have been measured in a small protein, mesoporphyrin-horseradish peroxidase via their influence on spectral diffusion broadening of holes burnt in the fluorescence excitation spectrum of free base mesoporphyrin. Holes were burnt in three 0----0 bands of different tautomeric forms of the chromophore at 1.5 and 4 K, and the spectral diffusion broadening was measured in temperature cycling experiments between 4 and 30 K. The inhomogeneous linewidth for the tautomeric 0----0 bands was estimated to be 60-70 cm-1; the hole width was found narrow, being in the order of 350 MHz (10(-2) cm-1) at 1.5 K what allowed for an extremely sensitive det…
Photochemical holes under pressure: Compressibility and volume fluctuations of a protein
From the pressure induced frequency shift of photochemical holes burnt into mesomorphyrin substituted horseradish peroxidase, we determined the compressibility of the protein and the vacuum frequency of the chromophore. From the compressibility, an estimation of the volume fluctuations of the biomolecule is possible.