Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Binding Sites
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Biological Transport
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Cell Compartmentation
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Copper / chemistry*
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Copper / metabolism
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Cysteine / chemistry
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Cysteine / metabolism
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Cytosol / chemistry
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Cytosol / metabolism
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Eukaryotic Cells / chemistry
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Eukaryotic Cells / metabolism
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Humans
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Ligands
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Metalloproteins / chemistry*
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Metalloproteins / metabolism
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Methionine / chemistry
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Methionine / metabolism
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Models, Molecular
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Sulfides / chemistry*
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Sulfides / metabolism
Substances
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Ligands
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Metalloproteins
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Sulfides
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Copper
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Methionine
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Cysteine