Metalloproteins


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Metalloproteins

 

a class of compound proteins, complexes of proteins with metal ions.

As a rule, the bond between the protein and the metal (for example, iron, copper, zinc, magnesium, manganese, vanadium, molybdenum) is weak; nonetheless, removal of the metal (for example, with inorganic acids) destroys the structure and functional properties of the complex. Metalloproteins are widely distributed in nature and perform important biological functions, such as oxygen transport in invertebrates (hemerythrin, hemocyanin), iron storage and transport (ferritin, transferritin), and copper storage and transport (ceruloplasmin). The group includes numerous enzymes (for example, certain peptidases, tyrosinase, and aspartic acid oxidase).

REFERENCES

Haurowitz, F. Khimiia i funktsiia belkov. Moscow, 1965. (Translated from English.)
Severin, S. E., P. P. Filippov, and G. A. Kochetov. “Metalloenzimy.” Uspekhi sovremennoi biologii, 1970, vol. 69, issue 2.
Vallee, B. L., and W. E. C. Wacker. “Metalloproteins.” In The Proteins, vol. 5. Edited by H. Neurath. New York-London, 1970.
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Metallothionein-like metalloproteins in the Baltic clam Macoma baltica: seasonal variations and induction upon metal exposure.
Bertini I, Sigel A, Sigel H, (2001) Handbook on Metalloproteins.
In various infections, cysteine-containing proteins, metalloproteins, calcium transport systems, (34) as well as essential enzymes of energy metabolism (35) have been identified as important intracellular targets for the toxic actions of peroxynitrite.
This text for students with a background in the life sciences or related fields serves as an introduction to biomolecular EPR spectroscopy, its basic principles, theory, and applications, including low-spin and high-spin metalloproteins, spin traps and labels, interaction between active sites, and redox systems.
SOD previously known as erythrocuprein (human) or hemocuprein (bovine), exists as a family of metalloproteins and is widely distributed in mammalian tissues (8,9).

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