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Respiratory pigment
A molecule that increases the oxygen-carrying capacity of blood

A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O2 transport. Other functions performed include O2 storage, CO2 transport, and transportation of substances other than respiratory gases. There are four major classifications of respiratory pigment: hemoglobin, hemocyanin, erythrocruorin–chlorocruorin, and hemerythrin. The heme-containing globin is the most commonly-occurring respiratory pigment, occurring in at least 9 different phyla of animals.

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Comparing Respiratory Pigments

MetalloproteinGlobinsHemocyaninHemerythrin
Hemoglobin4Erythrocruorin and chlorocruorin
O2 Binding MaterialIron5Iron6Copper7Iron8
LocationIntracellular9Extracellular10Extracellular11Intracellular12
Source OrganismAlmost all vertebrates13
  • Annelids and arthropods
  • Chlorocruorin: 4 families of marine polychaetes14
Arthropoda and Mollusca15

Sipuncula, priapulida, some brachiopoda, and a single annelid genus 16

Oxygenated ColorBright red17
  • Erythrocruorin: Bright red
  • Chlorocruorin: Green when diluted, red when concentrated 18
Blue19Violet20
Deoxygenated ColorCrimson21
  • Erythrocruorin: Dark red
  • Chlorocruorin: Green when diluted, brown-red when concentrated
Colorless22Colorless23

Hemoglobin, erythrocruorin, and chlorocruorin are all globins, iron-heme proteins with a common core. Their color comes from the absorption spectra of heme with Fe2+. Erythrocruorin and chlorocruorin are closely related giant globins found used by some invertebrates. Chlorocruorin has a special heme group, giving it different colors.

Any of various coloured conjugated proteins, such as hemoglobin, occur in living organisms and function in oxygen transfer in cellular respiration.

Globins

The globin is thought to be a very ancient molecule, even acting as a molecular clock of sorts. It has even been used to date the separation of vertebrates and invertebrates more than 1 billion years ago. Globin enjoys a large biological distribution, not only occurring among more than 9 different phyla of animals but occurring in some fungi and bacteria as well, even being identified in nitrogen-fixing nodules on the roots of some leguminous plants. The isolation of the globin gene from plant root cells has suggested that the globin genes that were inherited from a common ancestor shared by plants and animals may be present in all plants.24

Vertebrate hemoglobin

Vertebrates use a tetrameric hemoglobin, carried in red blood cells, to breathe. There are multiple types of hemoglobin that have been found in the human body alone. Hemoglobin A is the “normal” hemoglobin, the variant of hemoglobin that is most common after birth. Hemoglobin A2 is a minor component of hemoglobin found in red blood cells. Hemoglobin A2 makes up less than 3% of total red blood cell hemoglobin. Hemoglobin F typically is only found in the fetal stage of development. While Hemoglobin F falls dramatically after birth, it is possible for some people to produce some levels of Hemoglobin F throughout their full life.25

Other animal hemoglobins

Further information: Hemoglobin § Analogues in non-vertebrate organisms

Animals use a great variety of globins for respiration. By structure, they can be classified as:26: Fig. 1 

  • Intracellular Hbs. These globins reside inside a cell, much like the vertebrate Hb.
  • Multi-subunit Hbs. These globins form complexes and work outside a cell.
  • Multi-domain, multisubunit Hbs. These globins form complexes, work outside a cell, and have multiple globin domains per peptide chain.

Erythrocruorin and chlorocruorin belong to the multisubunit Hbs, specifically of the 12-dodecamer type.

Leghemoglobin

See also: phytoglobin

Leghemoglobin is a molecular similar in structure to myoglobin that is currently being used in artificial meat products, such as the Impossible Burger, to simulate both the color and taste of meat.27 Similar in function to hemoglobin, leghemoglobin contains trace amounts of iron, but it is primarily found in plant roots.28

Hemocyanin

Hemocyanin is a respiratory pigment that uses copper as its oxygen-binding molecule, as opposed to iron with hemoglobin. Hemocyanin is found in both arthropods and Mollusca, however it is thought that the molecule independently evolved in both phyla. There are several other molecules that exist in arthropods and Mollusca that are similar in structure to hemocyanin but serve entirely different purposes. For example, there are copper-containing tyrosinases that play significant roles in immune defense, wound healing, and the arthropod's cuticle. Molecules similar to hemocyanin in structure are grouped in under the hemocyanin superfamily.29

Notes

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Further reading

References

  1. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  2. also known as "hemoglobin", in a lax sense ↩

  3. Hill, Richard W.; Wyse, Gordon A.; Anderson, Margaret (5 October 2017). Transport of Oxygen and Carbon Dioxide in Body Fluids (with an Introduction to Acid–Base Physiology). Sinauer Associates. ISBN 978-1605357379. Archived from the original on 1 November 2020. Retrieved 10 November 2020. {{cite book}}: |website= ignored (help) 978-1605357379 ↩

  4. in the strict sense, for the tetrameric form ↩

  5. Lamy, Jean; Truchot, J.-P; Gilles, R; International Union of Biological Sciences; Section of Comparative Physiology and Biochemistry; International Congress of Comparative Physiology and Biochemistry, eds. (1985). Respiratory pigments in animals: relation, structure-function. Berlin; New York: Springer-Verlag. ISBN 978-0-387-15629-3. OCLC 12558726. 978-0-387-15629-3 ↩

  6. Fox, H. Munro (1949). "On Chlorocruorin and Haemoglobin". Proceedings of the Royal Society of London. Series B, Biological Sciences. 136 (884): 378–388. Bibcode:1949RSPSB.136..378F. doi:10.1098/rspb.1949.0031. ISSN 0080-4649. JSTOR 82565. PMID 18143368. S2CID 6133526. https://www.jstor.org/stable/82565 ↩

  7. Lamy, Jean; Truchot, J.-P; Gilles, R; International Union of Biological Sciences; Section of Comparative Physiology and Biochemistry; International Congress of Comparative Physiology and Biochemistry, eds. (1985). Respiratory pigments in animals: relation, structure-function. Berlin; New York: Springer-Verlag. ISBN 978-0-387-15629-3. OCLC 12558726. 978-0-387-15629-3 ↩

  8. Lamy, Jean; Truchot, J.-P; Gilles, R; International Union of Biological Sciences; Section of Comparative Physiology and Biochemistry; International Congress of Comparative Physiology and Biochemistry, eds. (1985). Respiratory pigments in animals: relation, structure-function. Berlin; New York: Springer-Verlag. ISBN 978-0-387-15629-3. OCLC 12558726. 978-0-387-15629-3 ↩

  9. Hill, Richard W.; Wyse, Gordon A.; Anderson, Margaret (5 October 2017). Transport of Oxygen and Carbon Dioxide in Body Fluids (with an Introduction to Acid–Base Physiology). Sinauer Associates. ISBN 978-1605357379. Archived from the original on 1 November 2020. Retrieved 10 November 2020. {{cite book}}: |website= ignored (help) 978-1605357379 ↩

  10. Fox, Harold Munro; Gardiner, John Stanley (1932-09-01). "The oxygen affinity of chlorocruorin". Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character. 111 (772): 356–363. doi:10.1098/rspb.1932.0060. https://doi.org/10.1098%2Frspb.1932.0060 ↩

  11. Hill, Richard W.; Wyse, Gordon A.; Anderson, Margaret (5 October 2017). Transport of Oxygen and Carbon Dioxide in Body Fluids (with an Introduction to Acid–Base Physiology). Sinauer Associates. ISBN 978-1605357379. Archived from the original on 1 November 2020. Retrieved 10 November 2020. {{cite book}}: |website= ignored (help) 978-1605357379 ↩

  12. Hill, Richard W.; Wyse, Gordon A.; Anderson, Margaret (5 October 2017). Transport of Oxygen and Carbon Dioxide in Body Fluids (with an Introduction to Acid–Base Physiology). Sinauer Associates. ISBN 978-1605357379. Archived from the original on 1 November 2020. Retrieved 10 November 2020. {{cite book}}: |website= ignored (help) 978-1605357379 ↩

  13. Hill, Richard W.; Wyse, Gordon A.; Anderson, Margaret (5 October 2017). Transport of Oxygen and Carbon Dioxide in Body Fluids (with an Introduction to Acid–Base Physiology). Sinauer Associates. ISBN 978-1605357379. Archived from the original on 1 November 2020. Retrieved 10 November 2020. {{cite book}}: |website= ignored (help) 978-1605357379 ↩

  14. Imai, Kiyohiro; Yoshikawa, Shinya (1985). "Oxygen-binding characteristics of Potamilla chlorocruorin". European Journal of Biochemistry. 147 (3): 453–463. doi:10.1111/j.0014-2956.1985.00453.x. ISSN 1432-1033. PMID 3979380. /wiki/Doi_(identifier) ↩

  15. Hill, Richard W.; Wyse, Gordon A.; Anderson, Margaret (5 October 2017). Transport of Oxygen and Carbon Dioxide in Body Fluids (with an Introduction to Acid–Base Physiology). Sinauer Associates. ISBN 978-1605357379. Archived from the original on 1 November 2020. Retrieved 10 November 2020. {{cite book}}: |website= ignored (help) 978-1605357379 ↩

  16. Lamy, Jean; Truchot, J.-P; Gilles, R; International Union of Biological Sciences; Section of Comparative Physiology and Biochemistry; International Congress of Comparative Physiology and Biochemistry, eds. (1985). Respiratory pigments in animals: relation, structure-function. Berlin; New York: Springer-Verlag. ISBN 978-0-387-15629-3. OCLC 12558726. 978-0-387-15629-3 ↩

  17. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  18. Fox, Harold Munro; Gardiner, John Stanley (1932-09-01). "The oxygen affinity of chlorocruorin". Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character. 111 (772): 356–363. doi:10.1098/rspb.1932.0060. https://doi.org/10.1098%2Frspb.1932.0060 ↩

  19. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  20. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  21. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  22. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  23. Urich, Klaus (1994), Urich, Klaus (ed.), "Respiratory Pigments", Comparative Animal Biochemistry, Berlin, Heidelberg: Springer, pp. 249–287, doi:10.1007/978-3-662-06303-3_7, ISBN 978-3-662-06303-3, retrieved 2020-11-21 978-3-662-06303-3 ↩

  24. Glomski, Chester; Tamburlin, Judith (1989). "The phylogenetic odyssey of the erythrocyte. I Hemoglobin: the universal respiratory pigment" (PDF). Histol Histopath. 4 (4): 509–514. PMID 2520483. https://digitum.um.es/digitum/bitstream/10201/18688/1/The%20phylogenetic%20odyssey%20of%20the%20erythrocyte.%20I%20Hemoglobin%20the%20universal%20respiratory%20pigment.pdf ↩

  25. "Hemoglobinopathies". sickle.bwh.harvard.edu. Retrieved 2020-11-21. https://sickle.bwh.harvard.edu/hemoglobinopathy.html ↩

  26. Weber RE, Vinogradov SN (April 2001). "Nonvertebrate Hemoglobins: Functions and Molecular Adaptations". Physiological Reviews. 81 (2): 569–628. doi:10.1152/physrev.2001.81.2.569. PMID 11274340. S2CID 10863037. /wiki/Doi_(identifier) ↩

  27. Lee, Hyun Jung; Yong, Hae In; Kim, Minsu; Choi, Yun-Sang; Jo, Cheorun (October 2020). "Status of meat alternatives and their potential role in the future meat market — A review". Asian-Australasian Journal of Animal Sciences. 33 (10): 1533–1543. doi:10.5713/ajas.20.0419. ISSN 1011-2367. PMC 7463075. PMID 32819080. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7463075 ↩

  28. Seehafer, A., & Bartels, M. (2019). Meat 2.0 the regulatory environment of plant-based and cultured meat. European Food and Feed Law Review (EFFL), 14(4),323-331. ↩

  29. Burmester, Thorsten (2001-02-01). "Molecular Evolution of the Arthropod Hemocyanin Superfamily". Molecular Biology and Evolution. 18 (2): 184–195. doi:10.1093/oxfordjournals.molbev.a003792. ISSN 0737-4038. PMID 11158377. https://academic.oup.com/mbe/article/18/2/184/1079272 ↩