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Open Access Articles- Top Results for Chlorocruorin

Chlorocruorin

File:Chlorocruorin.svg
Chlorocruorin.

Chlorocruorin is an oxygen-binding hemeprotein present in the blood plasma of many annelids, particularly certain marine polychaetes.[1][2][3] Its affinity for oxygen is weaker than that of most haemoglobins. A dichromatic compound, chlorocruorin is noted for appearing green in dilute solutions, though it appears light red when found in concentrated solutions.[4][5][6]

Its structure is very similar to erythrocruorin (which is likewise very similar to multiple subunits of myoglobin) and it contains many 16-17kDa myoglobin-like subunits arranged in a giant complex of over a hundred subunits with interlinking proteins as well with a total weight exceeding 3600kDa. The only significant difference between chlorocruorin and erythrocruorin is that chlorocruorin carries an abnormal heme group structure.[7] This enormous macromolecule is typically found free floating in the plasma, and not contained within red blood cells.[7][8]

References

  1. ^ H. Munro Fox (1 April 1933). "The Blood Circulation of Animals Possessing Chlorocruorin". Proceedings of the Royal Society B 112 (779): 479–495. JSTOR 81599. doi:10.1098/rspb.1938.0042. 
  2. ^ R. F. Ewer, H. Munro Fox (9 August 1940). "On the Function of Chlorocruorin". Proceedings of the Royal Society B 129 (855): 137–153. JSTOR 82389. doi:10.1098/rspb.1940.0033. 
  3. ^ D.W. Ewer (1941). "The blood systems of Sabella and Spirographis". Quarterly Journal of Microscopical Science 82 (s2): 587–619. Retrieved 1 May 2010. 
  4. ^ H. Munro Fox (1 February 1926). "Chlorocruorin: A Pigment Allied to Haemoglobin". Proceedings of the Royal Society B 99 (696): 199–220. JSTOR 81088. doi:10.1098/rspb.1926.0008. 
  5. ^ H. Munro Fox (1 September 1932). "The Oxygen Affinity of Chlorocruorin". Proceedings of the Royal Society B 111 (772): 356–363. JSTOR 81716. doi:10.1098/rspb.1932.0060. 
  6. ^ H. Munro Fox (19 October 1949). "On Chlorocruorin and Haemoglobin". Proceedings of the Royal Society B 136 (884): 378–388. JSTOR 82565. doi:10.1098/rspb.1949.0031. 
  7. ^ a b Pallavicini A, Negrisolo E, Barbato R et al. (July 2001). "The primary structure of globin and linker chains from the chlorocruorin of the polychaete Sabella spallanzanii". J. Biol. Chem. 276 (28): 26384–90. PMID 11294828. doi:10.1074/jbc.M006939200. 
  8. ^ Lamy JN, Green BN, Toulmond A, Wall JS, Weber RE, Vinogradov SN (19 December 1996). "Giant Hexagonal Bilayer Hemoglobins". Chem Rev 96 (8): 3113–3124. PMID 11848854. doi:10.1021/cr9600058. 

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