期刊
NATURE CHEMICAL BIOLOGY
卷 4, 期 2, 页码 107-109出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.2007.57
关键词
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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 Met(2)His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi 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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