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Cluster silver-amino acid

Class I and/or II MTs have been described in all animals examined. Mammalian MTs have been some of the most extensively studied of the 61 or 62 amino acids, 20 are cysteine residues. Metal ions are bound to the MT exclusively through thiolate bonds involving all 20 cysteines (see Hamer, 1986). They associate with a wide range of metals in vitro, 18 different metals in the case of rat liver MT (Nielson etal., 1985). Divalent and trivalent metals exhibit saturation binding at 7 mole equivalents forming M7-MT, whereas copper (Cu(I)) and silver (Ag(I)) bind as monovalent ions forming M12-MT. The structure of these molecules is such that two metal-binding domains are formed an a-cluster from the carboxy-terminal portion of the protein, contains 11 cysteines which bind either 4 divalent or 6 monovalent ions the (3-cluster, the amino-terminal... [Pg.3]

FIGURE 72.3. Molecular organization of arrAB (periplasmic arsenate reductase) and arsDABC (cytoplasmic arsenate reductase) of Shewanella strain ANA-3 (from GenBank Accession no. AY271310). arrAB gene cluster is located upstream in the opposite orientation to an arsDABC. aa-amino acid (modified Ifom Saltikov and Newman, 2003 Silver and Phung, 2005). [Pg.1086]


See other pages where Cluster silver-amino acid is mentioned: [Pg.317]    [Pg.320]    [Pg.326]    [Pg.159]    [Pg.81]    [Pg.81]    [Pg.239]    [Pg.122]    [Pg.136]   
See also in sourсe #XX -- [ Pg.212 ]




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