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- W2341886455 abstract "Metal ions play essential roles in about one third of enzymes [1]. These ions can modify electron flow in a substrate or enzyme, thus effectively controlling an enzyme-catalyzed reaction. They can serve to bind and orient substrate with respect to functional groups in the active site, and they can provide a site for redox activity if the metal has several valence states. Without the appropriate metal ion, a biochemical reaction catalyzed by a particular metalloenzyme would proceed very slowly, if at all. The enzyme provides an arrangement of sidechain functional groups having an appropriate sized hole with the preferred groups on enzyme side chains needed to bind the required metal ion. The optimal number of such binding groups is chosen for the particular metal ion, together with the appropriate hydrophobic or hydrophilic environment in the binding site. Metal ions may be bound by main-chain amino and carbonyl groups, but specific binding is achieved by the amino acid side chains, particularly the carboxylate groups of aspartic and glutamic acid, and the ring nitrogen atom of histidine. Other side chains that bind metals ions include tryptophan (ring nitrogen), cysteine (thiol), methionine (thioether), serine, threonine, tyrosine (hydroxyl groups), and asparagine and glutamine (carbonyl groups, less often amino groups)." @default.
- W2341886455 created "2016-06-24" @default.
- W2341886455 date "1989-07-01" @default.
- W2341886455 modified "2023-09-26" @default.
- W2341886455 title "Metal Ions in Biological Systems" @default.
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- W2341886455 doi "https://doi.org/10.1016/0223-5234(89)90095-0" @default.
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