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Haemoglobin Hiroshima and the Mechanism of the Alkaline Bohr Effect

Nature New Biology volume 232, pages 147–149 (1971)Cite this article

Abstract

HAEMOGLOBIN Hiroshima is a variant with interesting physiological properties1,2 discovered in a Japanese family. Its Bohr effect is halved, its oxygen affinity at physiological pH increased about three-fold, and haem-haem interaction is somewhat reduced compared with normal haemoglobin. In 0.1 M NaCl solutions initially stripped of phosphate, 2,3-diphospho-glycerate (2,3-DPG) diminishes the oxygen affinity as in haemoglobin A (H. F. Bunn, unpublished results). The amino-acid substitution originally deduced for this abnormal haemoglobin was histidine 143 (H21)β ⇐ aspartic acid1. It was possible to conceive of a mechanism which accounted for its diminished Bohr effect3, but the normal response of its oxygen affinity to 2,3-DPG was inconsistent with the proposed role of histidine 143 in 2,3-DPG binding by haemoglobin A4,5. An X-ray crystallographic study of deoxyhaemoglobin Hiroshima has now revealed that the replacement occurs not in position 143 but 146β. This was confirmed by chemical methods, and the physiological properties of this haemoglobin are now satisfactorily accounted for. The results support the role of histidine 146β in the alkaline Bohr effect6.

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Author information

Author notes

  1. S. SHIBATA

    Present address: Department of Medicine, Kawasaki Medical College Hospital, Nakasange, Okayama, Japan

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Cambridge

    M. F. PERUTZ, P. DEL PULSINELLI, L. TEN EYCK & J. V. KILMARTIN

  2. Department of Clinical Pathology, Kawasaki Hospital, Okayama

    S. SHIBATA & I. ÍUCHI

  3. Third Division of Internal Medicine, Yamaguchi University School of Medicine, Ube

    T. MIYAJI

  4. Department of Clinical Laboratories, Atomic Bomb Casualty Commission, Hiroshima

    H. B. HAMILTON

Authors
  1. M. F. PERUTZ
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  2. P. DEL PULSINELLI
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  3. L. TEN EYCK
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  4. J. V. KILMARTIN
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  5. S. SHIBATA
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  6. I. ÍUCHI
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  7. T. MIYAJI
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  8. H. B. HAMILTON
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PERUTZ, M., PULSINELLI, P., EYCK, L. et al. Haemoglobin Hiroshima and the Mechanism of the Alkaline Bohr Effect. Nature New Biology 232, 147–149 (1971). https://doi.org/10.1038/newbio232147a0

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