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Human Hemoglobin α chain (grey and pink) β chain (green and yellow) with bound O2 1gzx

Drag the structure with the mouse to rotate

References, for further information on Hemoglobin

To the structures used here:

  • Baldwin (1980) "The crystal structure of human carbonmonoxy haemoglobin at 2.7A resolution", J. Mol. Biol. 136: 103. (1hco) PMID: 7373648
  • Fermi, Perutz, Shaanan, & Fourme (1984) "The crystal structure of human deoxy haemoglobin at 1.74A resolution", J. Mol. Biol. 175: 159. (3hhb)
  • Jotaro Igarashi, Kazuo Kobayashi and Ariki Matsuoka (2011) "A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification", J. Biol. Inorg. Chem. 16(4):599-609 (3aq9) PMID: 21298303

General treatments of Hb allostery:

  • Perutz (1970) "Stereochemistry of cooperative effects in haemoglobin", Nature 228: 726
  • Baldwin & Chothia (1979) "Haemoglobin. The structural changes related to ligand binding and its allosteric mechanism", J. Mol. Biol. 129: 175. link
  • Dickerson & Geis (1983) "Hemoglobin: Structure, Function, and Pathology", Benjamin/Cummings Publ., Menlo Park, CA
  • Perutz (1989) "Mechanisms of cooperativity and allosteric regulation in proteins", Quarterly Rev. of Biophys. 22: 139-236
  • Ackers, Doyle, Myers, & Daugherty (1992) "Molecular code for cooperativity in hemoglobin", Science 255: 54
  • Perutz, Fermi, Poyart, Pagnier, & Kister (1993) "A novel allosteric mechanism in haemoglobin: Structure of bovine deoxyhaemoglobin, absence of specific chloride binding sites, and origin of the chloride-linked Bohr Effect in bovine and human haemoglobin", J. Mol. Biol. 233: 536

Hb structures in other quaternary states or intermediates:

  • Silva, Rogers, & Arnone (1992) "A third quaternary structure of human hemoglobin A at 1.7A resolution", J. Biol. Chem. 267: 17248
  • Smith, Lattman, & Carter (1991) "The mutation β99 Asp-Tyr stabilizes Y - A new, composite quaternary state of human hemoglobin", Proteins: Struct., Funct., Genet. 10: 81
  • Liddington, Derewenda, Dodson, Hubbard, & Dodson (1992) "High resolution crystal structures and comparisons of T state deoxyhaemoglobin and two liganded T-state haemoglobins: T(α-oxy)haemoglobin and T(met)Haemoglobin", J. Mol. Biol. 228: 551

More information on hemoglobin

  • Perutz, M.F. (1978) Hemoglobin Structure and Respiratory Transport, Scientific American, volume 239, number 6.
  • Squires, J.E. (2002) Artificial Blood, Science 295, 1002.
  • Vichinsky, E. (2002) New therapies in sickle cell disease. Lancet 24, 629.

Content Donators

Currently (June 22, 2008) most all of the content of this page comes from three main sources of generously donated content. Their work has been imported into this page. In their order of appearance on the page:

  1. Content adapted with permission from Eric Martz's hemoglobin tutorial at http://molviz.org
  2. Content adapted with permission from David S. Goodsell and Shuchismita Dutta's Molecule of the Month on Hemoglobin http://mgl.scripps.edu/people/goodsell/pdb/pdb41/pdb41_1.html
  3. Content adapted with permission from Jane S. and David C. Richardson's http://kinemage.biochem.duke.edu/

Proteopedia Page Contributors and Editors (what is this?)

Eran Hodis, Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky, Eric Martz, Karl Oberholser, Tihitina Y Aytenfisu, Mark Hoelzer, Marc Gillespie, Ann Taylor, Hannah Campbell, Karsten Theis

DOI: https://dx.doi.org/10.14576/32.2583112 (?)
Citation: Hodis E, Sussman J L, Gillespie M, Martz E, Prilusky J, Berchansky A, Oberholser K, Harel M, Taylor A, 2016, "Hemoglobin", Proteopedia, DOI: https://dx.doi.org/10.14576/32.2583112
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