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

  • News and Views |

    Hydrogenases are very powerful biocatalysts for dihydrogen cleavage. Now, X-ray crystallography shows how [Fe]-hydrogenase requires ligand exchanges at the metal centre and significant molecular motions to open and close its active site to effectively transfer a hydride to an electrophilic organic substrate.

    • Yvain Nicolet
    Nature Catalysis 2, 481-482
  • News and Views |

    High-yield production of a functionally active mimic of particulate methane monooxygenase in Escherichia coli has been presented. Investigation of its catalytic mode clarifies the role of duroquinol in biomimetic methanol production.

    • Sunney I. Chan
    •  & Steve S.-F Yu
    Nature Catalysis 2, 286-287
  • Research Highlights |

    Formylglycine residues are important functional handles on native and synthetic proteins. The formation of these residues is mediated by a copper enzyme operating via a superoxo intermediate.

    • David Schilter
  • Research Highlights |

    Bacteria sense metal ions using proteins whose interactions with DNA are sensitive to metal ion availability and identity. Less competitive metal ions trigger protein–DNA binding only at high concentrations.

    • David Schilter