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.

Latest Research and Reviews

News and Comment

  • News and Views |

    Nitrogenase has the canonical ability to reduce N2 to NH3, but under certain conditions, either in vitro or in vivo, it has the additional capability to convert CO2 to CO and CO to light hydrocarbons.

    • Holger Dobbek
  • News and Views |

    Interfacing photosynthetic proteins and electrodes for investigating light-induced charge separation remains challenging. The discovery of a competing charge transfer pathway through the light-harvesting antenna defines new design requirements for electrode modification.

    • Marc M Nowaczyk
    •  & Nicolas Plumeré
  • News and Views |

    Nitric oxide (NO) has important functions in all forms of life and serves, for example, as a signalling molecule in mammals. Now, two complementary studies have uncovered how NO binds to blue copper proteins. This research suggests a mechanism by which NO could regulate the activity of blue copper proteins involved in denitrification.

    • Subhra Samanta
    •  & Nicolai Lehnert
    Nature Chemistry 8, 639–641
  • News and Views |

    Iron–sulfur metalloproteins are critical for electron transfer in bacterial metabolism, but most crystal structures are insufficient for their in-depth study. Now, acquisition of an iron–sulfur protein structure at ultra-high resolution enables detailed visualization of its electron distribution.

    • Louis Noodleman
  • Editorial |

    Nitric oxide (NO) is an important signalling molecule in biological systems, but it is unclear exactly how it interacts with some metalloproteins. Now, a collection of articles in this issue reveal how NO binds to proteins containing type-1 copper sites.