Metalloproteins

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 |

    The sensitivities of a set of bacterial metal-sensing transcriptional regulators explain how a protein, such as the cobalt chelatase CbiK, is metalated with its cognate metal in cells rather than mis-metalated with more tightly binding metals.

    • Deenah Osman
    • , Maria Alessandra Martini
    • , Andrew W. Foster
    • , Junjun Chen
    • , Andrew J. P. Scott
    • , Richard J. Morton
    • , Jonathan W. Steed
    • , Elena Lurie-Luke
    • , Thomas G. Huggins
    • , Andrew D. Lawrence
    • , Evelyne Deery
    • , Martin J. Warren
    • , Peter T. Chivers
    •  & Nigel J. Robinson
  • Research | | open

    Tetrathiomolybdate (TM) and Cu-ATPases, e.g. Wilson (WLN) protein, affect the efficacy of common anticancer drug cisplatin. Here, the authors show that TM generates a protein dimer with a WLN domain by expelling copper and provide insight into the synergy of TM and cisplatin in cancer chemotherapy.

    • Tiantian Fang
    • , Wanbiao Chen
    • , Yaping Sheng
    • , Siming Yuan
    • , Qiaowei Tang
    • , Gongyu Li
    • , Guangming Huang
    • , Jihu Su
    • , Xuan Zhang
    • , Jianye Zang
    •  & Yangzhong Liu
  • Research |

    Designed split ferredoxins, fused to protein fragments that associate under certain conditions such as the presence of rapamycin, enable transcriptional and post-translational control over electron transfer in Escherichia coli cells and lysates.

    • Joshua T. Atkinson
    • , Ian J. Campbell
    • , Emily E. Thomas
    • , Sheila C. Bonitatibus
    • , Sean J. Elliott
    • , George N. Bennett
    •  & Jonathan J. Silberg
  • Research |

    Rubinstein and colleagues report a structure of the obligate respiratory III2IV2 supercomplex from M. smegmatis, revealing two functionally relevant conformations of the cytochrome cc subunit and a SOD subunit that may detoxify reactive oxygen species.

    • Benjamin Wiseman
    • , Ram Gopal Nitharwal
    • , Olga Fedotovskaya
    • , Jacob Schäfer
    • , Hui Guo
    • , Qie Kuang
    • , Samir Benlekbir
    • , Dan Sjöstrand
    • , Pia Ädelroth
    • , John L Rubinstein
    • , Peter Brzezinski
    •  & Martin Högbom
  • Research | | open

    Marine woodborers can digest woody biomass without the help of gut microbiota but the mechanism has remained unclear. Here, the authors provide evidence that the woodborer’s respiratory protein hemocyanin plays a central role in wood digestion and may offer a route toward biorefining of woody plant biomass.

    • Katrin Besser
    • , Graham P. Malyon
    • , William S. Eborall
    • , Giovanni Paro da Cunha
    • , Jefferson G. Filgueiras
    • , Adam Dowle
    • , Lourdes Cruz Garcia
    • , Samuel J. Page
    • , Ray Dupree
    • , Marcelo Kern
    • , Leonardo D. Gomez
    • , Yi Li
    • , Luisa Elias
    • , Federico Sabbadin
    • , Shaza E. Mohamad
    • , Giovanna Pesante
    • , Clare Steele-King
    • , Eduardo Ribeiro de Azevedo
    • , Igor Polikarpov
    • , Paul Dupree
    • , Simon M. Cragg
    • , Neil C. Bruce
    •  & Simon J. McQueen-Mason

News and Comment

  • News and Views |

    Superoxide dismutase mimics can help regulate the levels of O2•− in the body, but typically rely on redox-active metals that are toxic in their free form. Now, a complex featuring a redox-active quinol moiety complexed to a redox-inactive zinc centre has been shown to catalyse O2•− dismutation.

    • Diane E. Cabelli
    Nature Chemistry 10, 1173-1175
  • News and Views |

    Artificial metalloenzymes generally consist of a synthetic (organo)metallic catalyst incorporated into a protein. Asymmetric catalysis by such metalloenzymes could result by virtue of the chiral protein environment. Now, redox-sensitive anchoring enables reversible incorporation of an iridium catalyst for transfer hydrogenation.

    • Jun Okuda
    Nature Catalysis 1, 639-640
  • News and Views |

    Metalloprotein activity can be tuned by altering first- and second-sphere interactions with the metal ion or ions. Here, a non-canonical haem axial ligand is introduced into a myoglobin variant, modulating both. The resulting enhancement of cyclopropanation activity illustrates the utility of expanding the suite of available amino acids for biocatalyst engineering.

    • Emily H. Edwards
    •  & Kara L. Bren
    Nature Catalysis 1, 565-566
  • News and Views |

    How the first metabolic network was organized to power a cell remains an enigma. Now, simple iron–sulfur peptides have been used to generate a pH-gradient across a protocell membrane by catalysing hydrogen peroxide reduction. This indicates that short peptides could have fulfilled the role of redox active metalloproteins in early life.

    • Saidul Islam
    •  & Matthew W. Powner
    Nature Catalysis 1, 569-570