Metalloproteins are proteins bound by at least one metal ion. Metal ions are usually coordinated by four sites consisting of the protein’s nitrogen, sulphur and/or oxygen atoms. In metalloenzymes, one of the coordination sites is labile. The chemistry of metals allows for a broader set of reactions, for instance as in redox reactions.

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News and Comment

  • Research Highlights |

    The combination of mass spectroscopy-based proteomics with molecular dynamics enables the in-depth study of metallothioneine-Zn(II) binding mechanisms, critical to cell homeostasis and Zn(II) ion buffering.

    • Colette Whitfield
  • News & Views |

    The ability to control the subtle differences in reaction mechanisms and outcomes is an aspiration of many synthetic chemists. Now protein evolution has enabled the control of selectivity for hydroamination reactions catalysed by gold-based artificial metalloenzymes by favouring dual-gold catalysis over monomeric catalysis.

    • Amanda G. Jarvis
    Nature Catalysis 4, 639-640
  • News & Views |

    Heme-containing proteins support a broad range of cellular functions. A new crystal structure explains how an integral-membrane heme lyase attaches the hydrophobic heme to soluble proteins.

    • Breann L. Brown
    •  & T. M. Iverson