Directing noble metal ion chemistry within a designed ferritin protein

Christopher A. Butts, Joe Swift, Seung Gu Kang, Luigi Di Costanzo, David W. Christiansen, Jeffery G. Saven, Ivan J. Dmochowski

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Human H ferritin (HuHF) assembles from 24 four-helix bundles to form an ∼500 kDa protein with an 8 nm internal cavity. HuHF provides a useful model for studying the transport of metal ions in solution to buried reaction sites in proteins. In this study, HuHF was redesigned to facilitate noble metal ion (Au3+, Ag+) binding, reduction, and nanoparticle formation within the cavity. Computationally determined amino acid substitutions were targeted at four external and four internal surface sites. A variant with a total of 96 cysteines and histidines removed from the exterior surface and 96 non-native cysteines added to the interior surface retained wild-type stability and structure, as confirmed by X-ray crystallography, and promoted the formation of silver or gold nanoparticles within the protein cavity. Crystallographic studies with HuHF variants provide insight into how ferritins control access of metal ions to interior residues that perform chemistry. © 2008 American Chemical Society.
    Original languageEnglish
    Pages (from-to)12729-12739
    Number of pages10
    JournalBiochemistry
    Volume47
    Issue number48
    DOIs
    Publication statusPublished - 2 Dec 2008

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