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. 1976 Nov;58(5):1107–1109. doi: 10.1172/JCI108562

Hemoglobin St. Louis [beta 28 (B10) Leu replaced by Gln]: crystal structure of the fully reduced (deoxy) form.

N L Anderson
PMCID: PMC333277  PMID: 993333

Abstract

The three-dimensional structure of fully reduced Hb St. Louis has been determined to 3.5 A resolution. The difference electron density map clearly shows the site of the mutation and the effects it produces. Glutamine B10 and histidine E7 (the distal histidine) swing towards each other and, between them, stabilize a water molecule in the normally hydrophobic heme pocket. This creation of an aqueous microenvironment near the heme accounts for the thermal instability, high rate of methemoglobin formation, and increased oxygen affinity observed in solution studies of the mutant as described in the preceeding paper. Other than a small increase in tilt of the heme, virtually no further stereochemical disturbances result.

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Selected References

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  1. Cohen-Solal M., Seligmann M., Thillet J., Rosa J. Haemoglobin Saint Louis beta28 (B10) leucine leads to glutamine. A new unstable haemoglobin only present in a ferri form. FEBS Lett. 1973 Jun 15;33(1):37–41. doi: 10.1016/0014-5793(73)80153-x. [DOI] [PubMed] [Google Scholar]
  2. Misra H. P., Fridovich I. The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem. 1972 Nov 10;247(21):6960–6962. [PubMed] [Google Scholar]
  3. Perutz M. F., Lehmann H. Molecular pathology of human haemoglobin. Nature. 1968 Aug 31;219(5157):902–909. doi: 10.1038/219902a0. [DOI] [PubMed] [Google Scholar]
  4. Perutz M. F., Pulsinelli P. D., Ranney H. M. Structure and subunit interaction of haemoglobin M Milwaukee. Nat New Biol. 1972 Jun 28;237(78):259–263. doi: 10.1038/newbio237259a0. [DOI] [PubMed] [Google Scholar]
  5. Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Nature. 1970 Nov 21;228(5273):726–739. doi: 10.1038/228726a0. [DOI] [PubMed] [Google Scholar]
  6. Pulsinelli P. D., Perutz M. F., Nagel R. L. Structure of hemoglobin M Boston, a variant with a five-coordinated ferric heme. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3870–3874. doi: 10.1073/pnas.70.12.3870. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Thillet J., Cohen-Solal M., Seligmann M., Rosa J. Functional and physicochemical studies of hemoglobin St. Louis beta 28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron. J Clin Invest. 1976 Nov;58(5):1098–1106. doi: 10.1172/JCI108561. [DOI] [PMC free article] [PubMed] [Google Scholar]

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