Metalloproteins

A protein that has a metal ion cofactor is known as a "metalloprotein." This group includes a significant share of all proteins. There are up to 3000 human zinc metalloproteins, but at least 1000 human proteins have zinc-binding protein domains. According to estimates, a metal may be found in around half of all proteins. Another estimate suggests that between one-quarter and one-third of all proteins need metals to function. Consequently, metalloproteins serve a variety of purposes in cells, including the storage and movement of proteins, the transport and activity of enzymes and signalling proteins, and the prevention and treatment of infectious illnesses. The prevalence of metal-binding proteins may be innate to the amino acids that proteins employ since even synthetic proteins without evolutionary history will readily bind metals. Proteins hold the majority of metals in the human body. As an illustration, haemoglobin contains a significant amount of iron, which accounts for the body's relatively high concentration of iron. Typically, nitrogen, oxygen, or sulphur centres located in the protein's amino acid residues serve as the coordination centres for metal ions in metalloproteins. Side-chains on the residues of amino acids frequently act as these donor groups. The thiolate substitutes in cysteine residues, the carboxylate groups offered by aspartate, and the imidazole substitutes in histidine residues are particularly significant. The ability of almost all amino acid residues to bind metal centres has been demonstrated, which is a result of the diversity of the metalloproteome. Donor groups, such as deprotonated amides and amide carbonyl oxygen centers, are also provided by the peptide backbone.