Metalloproteins articles within Nature

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  • Article |

    Cryo-electron microscopy structures of the bacterial protein machinery that is involved in the production and function of nitrous oxide provide insight into the assembly pathway of this enzyme and the mechanisms of copper transport.

    • Christoph Müller
    • , Lin Zhang
    •  & Oliver Einsle

  • Article |

    X-ray crystal structures of TokK, a cobalamin- or B12-dependent radical SAM methylase, provide insight into how these enzymes use sequential radical-mediated methylations to assemble the C6 side chain of carbapenem antibiotics.

    • Hayley L. Knox
    • , Erica K. Sinner
    •  & Squire J. Booker

  • Letter |

    Hydrazine is an intermediate in the process of anaerobic ammonium oxidation which has a major role in the Earth’s nitrogen cycle; the crystal structure of a hydrazine synthase enzyme provides insights into the mechanism of hydrazine synthesis.

    • Andreas Dietl
    • , Christina Ferousi
    •  & Thomas R. M. Barends

  • Letter |

    Csp1, a novel copper-binding protein that is exported from the cytosol of the methanotroph Methylosinus trichosporium OB3b and stores copper ions for particulate methane monooxygenase, is identified and characterized.

    • Nicolas Vita
    • , Semeli Platsaki
    •  & Christopher Dennison

  • Letter |

    Sulfite-reducing microbes couple the reduction of sulfite to the generation of a proton motive force that sustains organismic growth; here, two X-ray crystal structures are solved of MccA, a c-type cytochrome enzyme with eight haem groups that catalyses the six-electron reduction of sulfite to sulfide at a novel haem–copper active site.

    • Bianca Hermann
    • , Melanie Kern
    •  & Oliver Einsle

  • Letter |

    The magnetosome-associated protein mamP is an iron oxidase that reveals a unique arrangement of a self-plugged PDZ domain fused to two magnetochrome domains, defining a new class of c-type cytochrome exclusively found in magnetotactic bacteria.

    • Marina I. Siponen
    • , Pierre Legrand
    •  & David Pignol

  • Letter |

    An X-ray structure of bacterial type VI secretion system components reveals that PAAR family proteins bind at the tip of the VgrG spike, providing new insights into the mechanisms of type VI secretion; experiments using bacteria confirmed the importance of PAAR proteins.

    • Mikhail M. Shneider
    • , Sergey A. Buth
    •  & Petr G. Leiman

  • Letter |

    Synchrotron-based nuclear resonance vibrational spectroscopy is used to characterize the reactive Fe(iv)=O intermediate of the halogenase SyrB2; the substrate directs the orientation of this intermediate, presenting specific frontier molecular orbitals that can activate the selective halogenation.

    • Shaun D. Wong
    • , Martin Srnec
    •  & Edward I. Solomon

  • Letter |

    Three synthetic mimics of the di-iron centre in [FeFe]-hydrogenases are loaded onto the HydF protein and then transferred to apo-HydA1; full activation of HydA1 was achieved only with the HydF hybrid protein that contained the mimic with an azadithiolate bridge, confirming the presence of this ligand in the active site of native [FeFe]-hydrogenases.

    • G. Berggren
    • , A. Adamska
    •  & M. Fontecave

  • Letter |

    The crystal structure of the complex between the hydroxylase and regulatory component of soluble methane monooxygenase is presented, revealing how the latter component controls substrate access to the hydroxylase active site.

    • Seung Jae Lee
    • , Michael S. McCormick
    •  & Uhn-Soo Cho

  • Letter |

    Metalloproteins are important in many biological processes, including respiration, photosynthesis and drug metabolism. Using genome sequences to predict the numbers and types of metal an organism uses is currently very challenging. These authors used a proteomics approach to identify and characterize a large number of a microorganism's metalloproteins on a genome-wide scale, and successfully separated and identified its cytoplasmic metalloproteins.

    • Aleksandar Cvetkovic
    • , Angeli Lal Menon
    •  & Michael W. W. Adams

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