Design of Multinuclear Gold Binding Site at the Two-fold Symmetric Interface of the Ferritin Cage

We have designed novel multinuclear metal-binding sites by introducing 96 Cys residues at the 2-fold symmetric interfaces in the protein cage of ferritin. X-ray crystal structure analysis showed that the introduced Cys coordinates to Au ions, forming a multinuclear gold-binding site. This study reve...

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Veröffentlicht in:Chemistry letters 2020-07, Vol.49 (7), p.840-844
Hauptverfasser: Hishikawa, Yuki, Maity, Basudev, Ito, Nozomi, Abe, Satoshi, Lu, Diannan, Ueno, Takafumi
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Sprache:eng
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Zusammenfassung:We have designed novel multinuclear metal-binding sites by introducing 96 Cys residues at the 2-fold symmetric interfaces in the protein cage of ferritin. X-ray crystal structure analysis showed that the introduced Cys coordinates to Au ions, forming a multinuclear gold-binding site. This study revealed that the robust cage structure contributes to fix the Cys residues introduced at the desired position and the ferritin subunit interface is a suitable site for constructing multinuclear metal-binding architectures.
ISSN:0366-7022
1348-0715
DOI:10.1246/cl.200217