Resonance Raman detection of structural dynamics at the active site in hemoglobin.

AUTOR(ES)

Ondrias, M R

RESUMO

The iron-histidine stretching mode in deoxyhemoglobin displays a large change in frequency and width upon lowering the temperature from 300 to 10 K. The temperature dependence of the data indicates the presence of dynamic process. The dynamics of this mode in frozen hemoglobins can be qualitatively and quantitatively described as a vibrational dephasing via anharmonic coupling to other vibrations of the heme-imidazole system. the effect that occur at the melting transition in the low frequency modes cannot be quantitatively addressed at this point but may be indicative of the introduction of additional degrees of freedom predicated on protein influences that reflect differences in protein quaternary structure.

Documentos Relacionados

• Mechanism of tertiary structural change in hemoglobin.
• Site-specific semisynthetic variant of human hemoglobin.
• Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin.
• Multiple conformations at functional site of hemerythrin: Evidence from resonance Raman spectra
• Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin.