Extremely weak linear electron-phonon coupling in iron-free hemeproteins studied by phase-modulated photon echo
- 1 October 1991
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review B
- Vol. 44 (14) , 7356-7361
- https://doi.org/10.1103/physrevb.44.7356
Abstract
The femtosecond accumulated photon echoes in iron-free myoglobin and iron-free cytochrome-C reveal that the linear electron-phonon coupling is extremely weak in these materials. This feature also manifests itself in the absence of the Stokes shift in the fluorescence spectrum over a wide range of temperatures from liquid-helium temperatures to near room temperatures. The origin of the weak coupling is attributed to the close packing of the porphyrin chromophores into a hydrophobic environment, which is constructed out of the polypeptide chain of the protein. The present results hint at the so-called hydrophobic compartmentalization of the chromophores as one of the important factors in reducing markedly the electron-phonon coupling in dye-polymer systems.Keywords
This publication has 17 references indexed in Scilit:
- Excited-state structure and energy-transfer dynamics of the bacteriochlorophyll a antenna complex from Prosthecochloris aestuariiThe Journal of Physical Chemistry, 1991
- Primary donor state mode structure and energy transfer in bacterial reaction centersThe Journal of Physical Chemistry, 1990
- Polymer dependence of boson peak frequency studied by hole burning and Raman spectroscopiesChemical Physics Letters, 1990
- Temperature dependence of Debye-Waller factor in dye-doped polymersPhysical Review B, 1990
- Persistent spectral hole-burning in heme proteins: Cytochrome c and myoglobinChemical Physics Letters, 1989
- Fourier-transform spectroscopy in dye-doped polymers using the femtosecond accumulated photon echoPhysical Review B, 1988
- Theory for spectral hole burning of the primary electron donor state of photosynthetic reaction centersBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- Site-selected fluorescence spectra of porphyrin derivatives of heme proteinsBiochemistry, 1985
- Sharp‐line structure in the fluorescence and excitation spectra of greening etiolated leavesFEBS Letters, 1984
- High-resolution optical studies on C-phycocyanin via photochemical hole burningJournal of the American Chemical Society, 1981