Thermal fluctuations between conformational substates of the Fe(2+)-HisF8 linkage in deoxymyoglobin probed by the Raman active Fe-N epsilon (HisF8) stretching vibration.

Ítems similars

• Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.
  per: Gilch, H., et al.
  Publicat: (1993)
• The Fe(2+)-His(F8) Raman band shape of deoxymyoglobin reveals taxonomic conformational substates of the proximal linkage.
  per: Schott, J, et al.
  Publicat: (2001)
• pH-induced conformational changes of the Fe(2+)-N epsilon (His F8) linkage in deoxyhemoglobin trout IV detected by the Raman active Fe(2+)-N epsilon (His F8) stretching mode.
  per: Bosenbeck, M., et al.
  Publicat: (1992)
• Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures.
  per: Nagai, K, et al.
  Publicat: (1980)
• Comments on the Article “Temperature Dependence of the Iron-Histidine Resonance Raman Band of Deoxyheme Proteins: Anharmonic Coupling Versus Distribution over Taxonomic Conformational Substates” by Korostishevsky et al.
  per: Dreybrodt, Wolfgang, et al.
  Publicat: (2004)