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.

Samankaltaisia teoksia

• Thermal fluctuations between conformational substates of the Fe(2+)-HisF8 linkage in deoxymyoglobin probed by the Raman active Fe-N epsilon (HisF8) stretching vibration.
  Tekijä: Gilch, H., et al.
  Julkaistu: (1995)
• 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.
  Tekijä: Bosenbeck, M., et al.
  Julkaistu: (1992)
• The Fe(2+)-His(F8) Raman band shape of deoxymyoglobin reveals taxonomic conformational substates of the proximal linkage.
  Tekijä: Schott, J, et al.
  Julkaistu: (2001)
• 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.
  Tekijä: Dreybrodt, Wolfgang, et al.
  Julkaistu: (2004)
• Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect
  Tekijä: Schweitzer-Stenner, Reinhard, et al.
  Julkaistu: (1993)