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Stereochemistry of cooperative effects in fish and amphibian haemoglobins

Nature volume 299, pages 421–426 (1982)Cite this article

Abstract

The low oxygen affinity of many fish haemoglobins at low pH is suggested to be due to the replacement by serine of the reactive cysteine F9β found in mammalian haemoglobins. Model building shows that hydrogen bonds between this serine and the C-terminal histidine stabilize the quaternary deoxy(T) structure. A stereochemical model for the binding of the allosteric effectors ATP or GTP is also advanced.

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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    M. F. Perutz

  2. Institute of Chemistry, Medicine, I University,

    M. Brunori

  3. Department of Biochemistry, Medicine, II University, Rome, Italy

    M. Brunori

Authors
  1. M. F. Perutz
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  2. M. Brunori
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Perutz, M., Brunori, M. Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature 299, 421–426 (1982). https://doi.org/10.1038/299421a0

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