Davis Anna V, O'Halloran Thomas V
Department of Chemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
Nat Chem Biol. 2008 Mar;4(3):148-51. doi: 10.1038/nchembio0308-148.
Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.
在过去十年中，半胱氨酸硫醇盐配体已被证明对于许多参与铜生理过程的胞质金属伴侣蛋白和金属调节蛋白的铜（I）（亚铜）结合化学至关重要。最近，甲硫氨酸的硫醚基团已开始成为在氧化性更强的细胞环境中用于转运蛋白的重要铜（I）配体。
