Cu(I) recognition via cation-π and methionine interactions in CusF
Y Xue, AV Davis, G Balakrishnan, JP Stasser… - Nature chemical …, 2008 - nature.com
Y Xue, AV Davis, G Balakrishnan, JP Stasser, BM Staehlin, P Focia, TG Spiro…
Nature chemical biology, 2008•nature.comMethionine-rich motifs have an important role in copper trafficking factors, including the
CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu (i) is
tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan.
Spectroscopic studies demonstrate that both thioether ligation and strong cation-π
interactions with tryptophan stabilize metal binding. This novel active site chemistry affords
mechanisms for control of adventitious metal redox and substitution chemistry.
CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu (i) is
tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan.
Spectroscopic studies demonstrate that both thioether ligation and strong cation-π
interactions with tryptophan stabilize metal binding. This novel active site chemistry affords
mechanisms for control of adventitious metal redox and substitution chemistry.
Abstract
Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-π interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
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