Structure, dynamics, and reactivity in hemoglobin

Research output: Contribution to journalArticle

119 Citations (Scopus)

Abstract

The static structure of hemoglobin and its functional properties are very well characterized. It is still not known how energy is stored and used within the structure of the protein to promote function and functional diversity. An essential part of this question is understanding the mechanism through which the overall protein structure (quaternary structure) couples to the local environment about the oxygen binding sites. Time-resolved resonance Raman spectroscopy has been used to probe the vibrational degrees of the freedom of the binding site as a function of protein structure. Comparison of the spectra from both equilibrium and transient forms of deoxy hemoglobin from a variety of mammalian, reptilian, and fish hemoglobins reveals that for each quaternary structure there exist two tertiary states stabilized by the presence or absence of an iron-bound ligand. Pulse-probe Raman experiments show that for photodissociated, ligated hemoglobins the local tertiary structure relaxes at a solution-dependent rate extending from tens of nanoseconds to microseconds. In this local environment, the linkage between the iron and the proximal histidine proves to be the single observed structural feature that responds in a systematic and substantial manner to structural changes in the protein. The additional finding of a correlation between the frequency of the iron-proximal histidine stretching motion (νFe-His) and various parameters of ligand reactivity, including geminate recombination, implicates the associated localized structural element in the mechanism of protein control of ligand binding. On the basis of these and related finds, a model is presented to account for both coarse and fine control of ligand binding by the protein structure.

Original languageEnglish (US)
Pages (from-to)1273-1280
Number of pages8
JournalScience
Volume228
Issue number4705
StatePublished - 1985
Externally publishedYes

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Hemoglobins
Ligands
Iron
Histidine
Quaternary Protein Structure
Proteins
Binding Sites
Raman Spectrum Analysis
Genetic Recombination
Carrier Proteins
Fishes
Oxygen

ASJC Scopus subject areas

  • General

Cite this

Structure, dynamics, and reactivity in hemoglobin. / Friedman, Joel M.

In: Science, Vol. 228, No. 4705, 1985, p. 1273-1280.

Research output: Contribution to journalArticle

Friedman, JM 1985, 'Structure, dynamics, and reactivity in hemoglobin', Science, vol. 228, no. 4705, pp. 1273-1280.
Friedman, Joel M. / Structure, dynamics, and reactivity in hemoglobin. In: Science. 1985 ; Vol. 228, No. 4705. pp. 1273-1280.
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