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

M. R. Ondrias, Denis L. Rousseau, S. R. Simon

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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 processes. 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 effects 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.

Original languageEnglish (US)
Pages (from-to)1511-1514
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number5
StatePublished - 1982
Externally publishedYes

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Catalytic Domain
Quaternary Protein Structure
Hemoglobins
Temperature
Vibration
Heme
Histidine
Freezing
Iron
Proteins
deoxyhemoglobin
imidazole

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Resonance Raman detection of structural dynamics at the active site in hemoglobin. / Ondrias, M. R.; Rousseau, Denis L.; Simon, S. R.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 79, No. 5, 1982, p. 1511-1514.

Research output: Contribution to journalArticle

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