Dynamics of hemoglobin investigated by Mössbauer spectroscopy

Journal of Biomolecular Structure & Dynamics
A LevyJ M Rifkind

Abstract

Mössbauer Spectra of Fe enriched horse hemoglobin and sperm whale myoglobin were measured in the temperature range from 80 K to 260 K. An analysis of the temperature dependence of the recoiless fraction (the Lamb-Mössbauer factor) shows it to be sensitive to conformational fluctuations which affect the mean square displacement of the iron. We have found that the protein conformation has a dramatic effect on these measurements. For hemoglobin greater conformational fluctuations at lower temperatures are observed for carbonmonoxyhemoglobin in the liganded conformation than for deoxyhemoglobin in the unliganded conformation. On the other hand, the Lamb-Mössbauer factor is insensitive to the binding of ligands to myoglobin and shows conformational fluctuations similar to deoxyhemoglobin even in the liganded state. It is also shown that a reversible complex with the distal histidine is formed in frozen deoxyhemoglobin solution above 200 K where the Lamb-Mössbauer factor shows the excitation of new modes of conformational fluctuations. This complex is not formed with carbonmonoxyhemoglobin which already has a sixth ligand and with deoxymyoglobin which appears to undergo much more limited conformational fluctuations. A possible relati...Continue Reading

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Citations

Jul 31, 1992·Biochimica Et Biophysica Acta·G ChottardG Herve
Nov 22, 1989·Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character·M N BartlettM C Symons

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