NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin.

@article{Lukin2000NMRRH,
  title={NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin.},
  author={Jonathan A Lukin and Virgil Simplaceanu and Ming qiang Zou and Nancy T. Ho and Chien Ho},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 19},
  pages={10354-8}
}
Compared with free heme, the proteins hemoglobin (Hb) and myoglobin (Mb) exhibit greatly enhanced affinity for oxygen relative to carbon monoxide. This physiologically vital property has been attributed to either steric hindrance of CO or stabilization of O(2) binding by a hydrogen bond with the distal histidine. We report here the first direct evidence of such a hydrogen bond in both alpha- and beta-chains of oxyhemoglobin, as revealed by heteronuclear NMR spectra of chain-selectively labeled… CONTINUE READING

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References

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Embryonic Encyclopedia of Life Sciences (Macmillan Reference, London)

C. Ho, J. A. Lukin
2000

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