Quaternary-transformation-induced changes at the heme in deoxyhemoglobins

M. R. Ondrias, Denis L. Rousseau, J. A. Shelnutt, S. R. Simon

Research output: Contribution to journalArticle

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Abstract

Quaternary-structure-induced differences in both the high- and low-frequency regions of the resonance Raman spectrum of the heme have been detected in a variety of hemoglobins. These differences may be the result of (1) changes in the amino acid sequence, induced by genetic and chemical modifications, and (2) alterations in the quaternary structure. For samples in solution in low ionic strength buffers, differences in the 1357-cm-1 line (an electron-density-sensitive vibrational mode) correlate with differences in the 216-cm-1 line (the iron-histidine stretching mode). Thus, changes in the iron-histidine bond and changes in the π-electron density of the porphyrin depend upon a common heme-globin interaction. The quaternary-structure-induced changes in the vibrational modes associated with the heme demonstrate that there is extensive communication between the heme and the globin and impact on models for the energetics of cooperativity. The local interactions of the iron-histidine mode are energetically small and destabilize the deoxy heme in the T structure with respect to the R structure. Therefore, these interactions must be larger in the ligated protein than in the deoxy protein to obtain a negative free energy of cooperativity. Additionally, our data imply that the deprotonation of the proximal histidine does not play a major role in the energetics of cooperativity. On the other hand, models for cooperativity that require conformational changes in the iron-histidine bond or direct interaction between the porphyrin and the protein are qualitatively consistent with the observed variation of heme electronic structure in concert with protein quaternary structure.

Original languageEnglish (US)
Pages (from-to)3428-3437
Number of pages10
JournalBiochemistry
Volume21
Issue number14
StatePublished - 1982
Externally publishedYes

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Heme
Histidine
Iron
Globins
Porphyrins
Carrier concentration
Quaternary Protein Structure
Proteins
Electrons
Deprotonation
Chemical modification
Ionic strength
Osmolar Concentration
Free energy
Stretching
Electronic structure
deoxyhemoglobin
Raman scattering
Amino Acid Sequence
Buffers

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ondrias, M. R., Rousseau, D. L., Shelnutt, J. A., & Simon, S. R. (1982). Quaternary-transformation-induced changes at the heme in deoxyhemoglobins. Biochemistry, 21(14), 3428-3437.

Quaternary-transformation-induced changes at the heme in deoxyhemoglobins. / Ondrias, M. R.; Rousseau, Denis L.; Shelnutt, J. A.; Simon, S. R.

In: Biochemistry, Vol. 21, No. 14, 1982, p. 3428-3437.

Research output: Contribution to journalArticle

Ondrias, MR, Rousseau, DL, Shelnutt, JA & Simon, SR 1982, 'Quaternary-transformation-induced changes at the heme in deoxyhemoglobins', Biochemistry, vol. 21, no. 14, pp. 3428-3437.
Ondrias, M. R. ; Rousseau, Denis L. ; Shelnutt, J. A. ; Simon, S. R. / Quaternary-transformation-induced changes at the heme in deoxyhemoglobins. In: Biochemistry. 1982 ; Vol. 21, No. 14. pp. 3428-3437.
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