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

  • Research | | open

    The biosynthesis of iron-sulfur clusters in anaerobic organisms has not been extensively investigated. Here, the authors identify and characterize a multi-subunit protein that stores iron and sulfur in thioferrate for the assembly of the clusters in Pyrococcus furiosus.

    • Brian J. Vaccaro
    • , Sonya M. Clarkson
    • , James F. Holden
    • , Dong-Woo Lee
    • , Chang-Hao Wu
    • , Farris L. Poole II
    • , Julien J. H. Cotelesage
    • , Mark J. Hackett
    • , Sahel Mohebbi
    • , Jingchuan Sun
    • , Huilin Li
    • , Michael K. Johnson
    • , Graham N. George
    •  & Michael W. W. Adams
  • Research |

    Current mineral-based theories do not fully address how enzymes emerged from prebiotic catalysts. Now, iron–sulfur clusters can be synthesized by UV-light-mediated photolysis of organic thiols and photooxidation of ferrous ions. Iron–sulfur peptides may have formed easily on early Earth, facilitating the emergence of iron–sulfur-cluster-dependent metabolism.

    • Claudia Bonfio
    • , Luca Valer
    • , Simone Scintilla
    • , Sachin Shah
    • , David J. Evans
    • , Lin Jin
    • , Jack W. Szostak
    • , Dimitar D. Sasselov
    • , John D. Sutherland
    •  & Sheref S. Mansy
  • Research |

    The oxidative prowess of cytochrome P450s has been suggested to stem from the electron-donating axial ligand. Now, a selenocysteine-ligated P450 compound I has been trapped and characterized providing an avenue to examine this hypothesis. Measurements reveal that the selenolate-ligated compound I cleaves C–H bonds more rapidly than the wild-type equivalent.

    • Elizabeth L. Onderko
    • , Alexey Silakov
    • , Timothy H. Yosca
    •  & Michael T. Green
    Nature Chemistry 9, 623–628
  • Research |

    The bicyclic disulfide–containing compound thiolutin has broad antimicrobial activity and targets the essential proteasomal deubiquitinase Rpn11 and other metalloproteases, leading to inhibition of enzymatic activity through a mechanism involving zinc chelation.

    • Linda Lauinger
    • , Jing Li
    • , Anton Shostak
    • , Ibrahim Avi Cemel
    • , Nati Ha
    • , Yaru Zhang
    • , Philipp E Merkl
    • , Simon Obermeyer
    • , Nicolas Stankovic-Valentin
    • , Tobias Schafmeier
    • , Walter J Wever
    • , Albert A Bowers
    • , Kyle P Carter
    • , Amy E Palmer
    • , Herbert Tschochner
    • , Frauke Melchior
    • , Raymond J Deshaies
    • , Michael Brunner
    •  & Axel Diernfellner
  • Research | | open

    The mitochondrial proteins ISCA1 and ISCA2 form a complex that is involved in the biogenesis of Fe–S clusters. Here the authors report that ISCA1 and ISCA2 interact differently with proteins of the Fe–S machinery and that under certain conditions, ISCA2 seems dispensable for Fe–S biogenesis.

    • Lena Kristina Beilschmidt
    • , Sandrine Ollagnier de Choudens
    • , Marjorie Fournier
    • , Ioannis Sanakis
    • , Marc-André Hograindleur
    • , Martin Clémancey
    • , Geneviève Blondin
    • , Stéphane Schmucker
    • , Aurélie Eisenmann
    • , Amélie Weiss
    • , Pascale Koebel
    • , Nadia Messaddeq
    • , Hélène Puccio
    •  & Alain Martelli

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
  • 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.

  • 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