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hemocyanins
Sign in to saveAlso known as haemocyanins, hemocyanin, haemocyanin
Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O2). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not confined in blood cells, but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygen
Key facts
- Protein family.Symbol
- Hemocyanin_C
- Protein family.Name
- Hemocyanin, ig-like domain
- Protein family.image
- PDB 1oxy EBI.jpg
- Protein family.caption
- Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 angstroms resolution
- Protein family.Pfam
- PF03722
- Protein family.InterPro
- IPR005203
- Protein family.Prosite
- PDOC00184
- Protein family.SCOP
- 1lla
- Protein family.PDB
- 110-373 :110-373 :110-373 110-373 A:136-393 D:136-393 B:136-393 C:136-393 C:136-393 C:136-393 C:136-393
- Protein family.PROSITE
- PDOC00184
via Wikipedia infobox
Wikidata facts
- Image
- Hemocyanin Example.jpg
Show 1 more fact
- Commons category
- Hemocyanin
Sources (2)
via Wikidata · CC0
~10 min read
Article
11 sectionsContents
- Species distribution
- The hemocyanin superfamily
- Structure and mechanism
- Catalytic activity
- Spectral properties
- Anticancer effects
- Case studies: environmental impact on hemocyanin levels
- See also
- References
- Further reading
- External links
Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O2). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not confined in blood cells, but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form.
== Species distribution == Hemocyanin was first discovered in Octopus vulgaris by Leon Fredericq in 1878. The presence of copper in molluscs was detected even earlier by Bartolomeo Bizio in 1833. Hemocyanins are found in the Mollusca and Arthropoda, including cephalopods and crustaceans, and utilized by some land arthropods such as the tarantula Eurypelma californicum, the emperor scorpion, and the centipede Scutigera coleoptrata. Also, larval storage proteins in many insects appear to be derived from hemocyanins.