TY - JOUR
T1 - A place for thioether chemistry in cellular copper ion recognition and trafficking
AU - Davis, Anna V.
AU - O'Halloran, Thomas V.
PY - 2008/3
Y1 - 2008/3
N2 - 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.
AB - 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.
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U2 - 10.1038/nchembio0308-148
DO - 10.1038/nchembio0308-148
M3 - Comment/debate
C2 - 18277969
AN - SCOPUS:39449113042
SN - 1552-4450
VL - 4
SP - 148
EP - 151
JO - Nature Chemical Biology
JF - Nature Chemical Biology
IS - 3
ER -