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.
References in periodicals archive ?
Metalloproteins (MT) were discovered by Margoshes and Valle (1957), who isolated them from the renal cortex of horses and identified them as proteins able to combine with cadmium (Cd).
Dudev, "Gallium as a Therapeutic Agent: A Thermodynamic Evaluation of the Competition between Ga3+ and Fe3+ Ions in Metalloproteins," The Journal of Physical Chemistry B, vol.
Redox potential reactions due to these metals, many give out important roles as cofactors in enzymes and about 30-45 per cent of known enzymes are metalloproteins which perform function under availability of metal co-factor (Klein and Lewinson 2011).
Heavy metals like Zn and Cu act either as activators for enzyme catalyzed reactions [3] or as prosthetic group in metalloproteins. As essential nutrients the heavy metals are required in redox reactions, electron transfer and also play structural roles in the metabolism of nucleic acids.
Cyclophilin A is also involved in the activation of matrix metalloproteins, which are chemoattractants for inflammatory cells (13, 14).
The loss of Thr and Lys could be due to the formation of intermediary adducts such as [alpha]-amino-3-keto butyric acid and [alpha]-amino adipic semialdehyde, as a consequence of oxidation catalyzed by metals from the metalloproteins of the food matrix [43].
These pathomechanisms include well-established oxidative stress, which is tightly bound to the incorrect generation of metalloproteins, the activation of microglial cells, and inflammation [146].
These biochemical mechanisms include the role of excitatory amino acids, caspases, protein kinases, oxygen free radicals, nitric oxide, tumor necrosis factor-alpha, neurotrophins, and metalloproteins [8].

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