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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Sep;70(9):2647–2650. doi: 10.1073/pnas.70.9.2647

Synthesis of the Myoglobin Active Site

C K Chang 1, T G Traylor 1,*
PMCID: PMC427074  PMID: 4517676

Abstract

A simple heme-imidazole compound, having the same geometry as the heme-imidazole complex in myoglobin, has been synthesized. This compound, ferropyrroporphyrin-N-[3-(1-imidazolyl)propyl]amide, reversibly binds oxygen in the solid state or when dissolved in a polystyrene film. These results suggest that the principal factors governing reversible oxygen binding are the electronic nature of the base (imidazole), neighboring-group effects of the basic group, and immobilization of the heme group.

Keywords: hemoglobin, oxyheme, heme-oxygen bond, neighboring group

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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