Spectral hole burning study of protoporphyrin IX substituted myoglobin

This publication has 15 references indexed in Scilit:

• More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. High resolution optical spectroscopic study
  Biophysical Journal, 1992
• Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase
  Biophysical Journal, 1991
• Conformational substates and motions in myoglobin. External influences on structure and dynamics
  Biophysical Journal, 1990
• Contributions of the electrostatic and the dispersion interaction to the solvent shift in a dye-polymer system, as investigated by hole-burning spectroscopy
  Physical Review B, 1990
• Glassy behavior of a protein
  Physical Review Letters, 1989
• Spectroscopic studies of impurity-host interactions in dye-doped polymers: Hydrostatic-pressure effects versus temperature effects
  Physical Review B, 1987
• Low temperature X-ray investigation of structural distributions in myoglobin
  European Biophysics Journal, 1987
• Conformation-Controlled Trans-Effect of the Proximal Histidine in Haemoglobins. An Electron Spin Resonance Study of Monomeric Nitrosyl-⁵⁷Fe-Haemoglobins
  Zeitschrift für Naturforschung C, 1976
• Thermodynamic fluctuations in protein molecules.
  Proceedings of the National Academy of Sciences, 1976
• Low temperature photodissociation of hemoproteins: Carbon monoxide complex of myoglobin and hemoglobin
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974