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Myoglobin

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Myoglobin 3D structure.
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Myoglobin 3D structure.

Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. It is the primary oxygen-carrying pigment of muscle tissues. Unlike the blood-borne hemoglobin, to which it is structurally related, this protein does not exhibit cooperative binding of oxygen. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen tension in the surrounding tissue. In 1957, John Kendrew and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallography.

For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.

See also hemoglobin, hemoprotein

External links

  • oxy-myoglobin at 0.1 nm resolution: PDB 1A6M (http://www.rcsb.org/pdb/cgi/explore.cgi?pid=105291034356398&page=0&pdbId=1A6M)
  • Sperm whale myoglobin at 0.17 nm resolution: PDB 1VXH (http://www.rcsb.org/pdb/cgi/explore.cgi?pid=255731034609024&page=80&pdbId=1VXH)

fr:Myoglobine

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This page was last modified 21:44, 22 Sep 2004.
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