Bioinorganic chemistry articles within Nature Communications

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  • Article
    | Open Access

    The inorganic minerals are believed to exert a critical catalytic role in the prebiotic time, but biominerals (e.g., bones) in modern living organisms are known mainly for their physical property-related functions. Here the authors identify natural ferritin iron core as a superoxide dismutase-like nanozyme exhibiting species-related activity and elucidate its specific catalytic mechanism.

    • Long Ma
    • , Jia-Jia Zheng
    •  & Kelong Fan

  • Article
    | Open Access

    The structure of vaterite has been debated for a century. Combining systematic TEM characterisations, crystallographic analysis, and machine learning aided molecular dynamics simulations, the authors unlock the structural mystery in vaterite.

    • Xingyuan San
    • , Junwei Hu
    •  & Xiaobing Hu

  • Article
    | Open Access

    TerC family membrane proteins associate with the general protein secretion complex to facilitate the co-translocational loading of Mn(II) into nascent metalloenzymes. Here, the authors show that Bacillus subtilis mutants lacking TerC proteins are defective in production of the membrane-embedded lipoteichoic acid synthase and secreted proteases.

    • Bixi He
    • , Ankita J. Sachla
    •  & John D. Helmann

  • Article
    | Open Access

    Rieske oxygenase chemistry is important for biochemical pathways, but it remains elusive how a common protein scaffold can be predictively tuned to catalyze divergent reactions. Here, the authors report a strategy that can rationally tune TsaM, a Rieske monooxygenase to catalyze dioxygenation and sequential monooxygenation reactions, and customize the reactivity of other Rieske oxygenases.

    • Jiayi Tian
    • , Jianxin Liu
    •  & Jennifer Bridwell-Rabb

  • Article
    | Open Access

    The development of dynamic DNA nanodevices, whose configuration and function are regulated by specific chemical inputs, represents a rapidly growing area in molecular science. Herein, the authors report the concept of metal-mediated base-pair switching to induce inter- and intramolecular DNA strand displacement in a metal-responsive manner.

    • Yusuke Takezawa
    • , Keita Mori
    •  & Mitsuhiko Shionoya

  • Article
    | Open Access

    Biological nitrogen fixation is achieved by nitrogenase, but the mechanism remains enigmatic. Here, the authors report high resolution single particle cryoEM structures of homocitrate-compromised MoFe-proteins and unveil a new binding partner.

    • Rebeccah A. Warmack
    • , Ailiena O. Maggiolo
    •  & Douglas C. Rees

  • Article
    | Open Access

    The characterization of nickel (Ni)‐centred paramagnetic states relevant to [NiFe] hydrogenases is rare in mononuclear Ni hydrogen evolution catalysts. Here, the authors report the spectroscopic and synthetic characterization of NiI and NiIII states in an organometallic Ni hydrogen evolution catalyst.

    • Sagnik Chakrabarti
    • , Soumalya Sinha
    •  & Liviu M. Mirica

  • Article
    | Open Access

    Metal-catalysed oxidation of proteins varies in selectivity and depends on the surface residues to direct the reaction. Here, the authors use polyoxometalate clusters as inorganic ligands for Cu ions, enabling the regioselective oxidative cleavage of a protein via reactive oxygen species in the vicinity of its binding sites.

    • Shorok A. M. Abdelhameed
    • , Francisco de Azambuja
    •  & Tatjana N. Parac-Vogt

  • Article
    | Open Access

    The enzyme ATE1 catalyzes eukaryotic post-translation arginylation, a key protein modification necessary for cellular homeostasis. Here, the authors show that ATE1s are previously unrealized iron-sulfur proteins that use this oxygen-sensitive inorganic cofactor to control cellular arginylation

    • Verna Van
    • , Janae B. Brown
    •  & Aaron T. Smith

  • Article
    | Open Access

    Electron transfer between mitochondrial cytochrome c and subunit of cytochrome bc1 can proceed at long distance. Here the authors investigate further the mechanism and show phosphorylation regulation of the interactions between the protein partners in the electron transport chain.

    • Alexandre M. J. Gomila
    • , Gonzalo Pérez-Mejías
    •  & Anna Lagunas

  • Article
    | Open Access

    The cytochrome P450 enzyme CYP1B1 is overexpressed in a variety of tumors, and is correlated with poor treatment outcomes; thus, it is desirable to develop CYP1B1 inhibitors to restore chemotherapy efficacy. Here the authors describe the creation of light-triggered CYP1B1 inhibitors as “prodrugs”, and achieve >6000-fold improvement in potency upon activation with low-energy (660 nm) light.

    • Dmytro Havrylyuk
    • , Austin C. Hachey
    •  & Edith C. Glazer

  • Article
    | Open Access

    Defect engineering of 2 dimensional layered double hydroxide sheets improves their photocatalytic activity. Here, the authors etch sheets in acid and show that the etched sheets generate substantially more reactive oxygen species that untreated sheets and the treated sheets can be used to kill cancer cells in vitro and in vivo.

    • Weicheng Shen
    • , Tingting Hu
    •  & Chaoliang Tan

  • Article
    | Open Access

    Molecules offer enormous capacity for information storage. Here, the authors show that information can be encoded into molecules with sequences of paramagnetic lanthanide ions, and decoded using nuclear magnetic resonance spectroscopy.

    • Jan Kretschmer
    • , Tomáš David
    •  & Miloslav Polasek

  • Article
    | Open Access

    Photodynamic therapy has been a promising technique for the treatment of tumours. In this manuscript, the authors report on the photoactivation of the osmium peroxo complex and its potential use for chemotherapy and photodynamic therapy under blue light irradiation against tumours in their hypoxic environment.

    • Nong Lu
    • , Zhihong Deng
    •  & Pingyu Zhang

  • Article
    | Open Access

    Modifying the reactivity of substrates by encapsulation is essential for microenvironment catalysts. Herein, the authors report an alternative strategy that modifies the entry behaviour of reactants and substrates to control the electron injection kinetics, thus affecting the selectivity of nitroarene photoreductions.

    • Yang Yang
    • , Xu Jing
    •  & Chunying Duan

  • Article
    | Open Access

    Dynamic control over protein function is a central challenge in synthetic biology. Here the authors present an integrated computational and experimental workflow for engineering reversible protein switches; metal-chelating unnatural amino acids genetically encoded into two conformationally dynamic enzymes to yield robust switches.

    • Yasmine S. Zubi
    • , Kosuke Seki
    •  & Jared C. Lewis

  • Article
    | Open Access

    Iron coordination complexes can be used to gain insight on biologically relevant iron-oxygen compounds generated in iron metalloenzymes. Here, the authors characterise a μ-1,2-hydroperoxo FeIIIFeIII and a μ-1,2-peroxo FeIVFeIII, and study their reactivity in C-H activation.

    • Stephan Walleck
    • , Thomas Philipp Zimmermann
    •  & Thorsten Glaser

  • Article
    | Open Access

    The “anti-branching rule”, introduced in 1950, excludes branched polyphosphates from biological relevance due to their supposedly rapid hydrolysis. Here, the authors synthesize monodisperse branched polyphosphates and demonstrate their unexpected stability in water, as well as provide evidence for their competence in phosphorylation.

    • Tobias Dürr-Mayer
    • , Danye Qiu
    •  & Henning J. Jessen

  • Article
    | Open Access

    Sonodynamic therapy has therapeutic promise due to its safety and good tissue penetration, but is currently bottlenecked due to a lack of efficient and safe sonosensitizers. Here the authors show that [Ru(bpy)3]2+ can produce singlet oxygen and sonooxidize NADH in deep tissue, and destroy mouse tumors effectively.

    • Chao Liang
    • , Jiaen Xie
    •  & Pingyu Zhang

  • Article
    | Open Access

    Heme biosynthesis depends on iron-sulfur (Fe-S) cluster biogenesis but the molecular connection between these pathways is not fully understood. Here, the authors show that the heme biosynthesis enzyme ALAD contains an Fe-S cluster, disruption of which reduces ALAD activity and heme production in human cells.

    • Gang Liu
    • , Debangsu Sil
    •  & Tracey Ann Rouault

  • Article
    | Open Access

    The sulfur-reducing enzyme MBS and the hydrogen-gas evolving MBH are the evolutionary link between the ancestor Mrp antiporter and the mitochondrial respiratory complex I. Here, the authors characterise MBS from the hyperthermophilic archaeon Pyrococcus furiosus, solve its cryo-EM structure and discuss the structural evolution from Mrp to MBH and MBS and to the modern-day complex I.

    • Hongjun Yu
    • , Dominik K. Haja
    •  & Michael W. W. Adams

  • Article
    | Open Access

    Photosensitizers that  are stable in biological conditions with absorption in the biological spectral window are needed for photodynamic therapy. Here, the authors report on the development of a Ruthenium complex for 1 and 2-photon therapy to address these issues and demonstrate application in vivo.

    • Johannes Karges
    • , Shi Kuang
    •  & Gilles Gasser

  • Article
    | Open Access

    Many metalloenzymes are highly specific for their cognate metal ion but the molecular principles underlying this specificity often remain unclear. Here, the authors characterize the structural and biochemical basis for the different metal specificity of two evolutionarily related superoxide dismutases.

    • Anna Barwinska-Sendra
    • , Yuritzi M. Garcia
    •  & Kevin J. Waldron

  • Article
    | Open Access

    Understanding enzyme active sites can elucidate fundamental enzymatic reaction pathways and inform designs for synthetic catalysts. Here, authors employ operando X-ray absorption spectroelectrochemistry to assess copper ions in bilirubin oxidase during oxygen reduction electrocatalysis.

    • Lucyano J. A. Macedo
    • , Ayaz Hassan
    •  & Frank N. Crespilho

  • Article
    | Open Access

    Mobile group II introns function as ribozymes to splice and reinsert themselves into DNA, thereby colonizing new genomic regions. Here the authors use single-molecule FRET and molecular dynamics simulations to reveal a structural link between metal ion induced kinetic heterogeneity and the sugar puckers at the exon-intron binding interface.

    • Fabio D. Steffen
    • , Mokrane Khier
    •  & Roland K. O. Sigel

  • Article
    | Open Access

    Iron is essential for growth of Mycobacterium tuberculosis, but most of the iron in the human body is stored in heme within hemoglobin. Here, Mitra et al. identify two heme uptake mechanisms in M. tuberculosis, one dependent on the inner-membrane Dpp importer and the other dependent on host albumin.

    • Avishek Mitra
    • , Ying-Hui Ko
    •  & Michael Niederweis

  • Article
    | Open Access

    Metallo-β-lactamases (MBLs) confer resistance to carbapenem antibiotics. Here, López et al. show that the host range of MBLs depends on the efficiency of MBL signal peptide processing and secretion into outer membrane vesicles, which affects bacterial fitness.

    • Carolina López
    • , Juan A. Ayala
    •  & Alejandro J. Vila

  • Article
    | Open Access

    The mechanism of iron-sulfur (Fe-S) cluster biosynthesis is not fully understood. Here, the authors develop a physiologically relevant in vitro model of Fe-S cluster assembly, allowing them to elucidate the sequence of Fe-S cluster synthesis along with the respective roles of ferredoxin-2 and frataxin.

    • Sylvain Gervason
    • , Djabir Larkem
    •  & Benoit D’Autréaux

  • Article
    | Open Access

    In vivo decorporation of U(VI) from bones is an unsolved challenge because of the formation of stable uranium phosphate complexes. Here, the authors develop a hydroxypyridonone-based ligand with strong uranium complexation and low cytotoxicity. They find this ligand effectively removes uranium from kidney and bones in mice, and is suitable for oral administration.

    • Xiaomei Wang
    • , Xing Dai
    •  & Shuao Wang

  • Article
    | Open Access

    The activity of the membrane-bound enzyme pMMO depends on copper but the location of the copper centers is still under debate. Here, the authors reconstitute pMMO in nanodiscs and use native top-down MS to localize its copper centers, providing insights into which sites are essential for activity.

    • Soo Y. Ro
    • , Luis F. Schachner
    •  & Amy C. Rosenzweig

  • Article
    | Open Access

    Studying the electronic structures and spin transitions of synthetic heme analogs is crucial to advancing our understanding of heme enzyme mechanisms. Here the authors show that a Co(II) porphyrin complex undergoes an unexpected spin state transition upon deprotonation of its axial imidazole ligand.

    • Jianping Zhao
    • , Qian Peng
    •  & Jianfeng Li

  • Article
    | Open Access

    The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods.

    • Kimberly Rizzolo
    • , Steven E. Cohen
    •  & Sean J. Elliott

  • Article
    | Open Access

    FeV(O)(OH) species have long been thought to play a role in a range of enzymatic oxidations, but their characterization has remained elusive. Here, using gas-phase ion spectroscopy, the authors characterize an FeV(O)(OH) species and find that its reactivity mimics that of Rieske oxygenases.

    • Margarida Borrell
    • , Erik Andris
    •  & Miquel Costas

  • Article
    | Open Access

    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
    •  & Yangzhong Liu

  • Article
    | Open Access

    Controlled switching of the spin state of transition metal ions is key in many enzymatic reactions, but difficult to replicate in synthetic systems. Here the authors report on an iron(III) porphyrin with a photochromic axial ligand that, in solution, reversibly switches between low-spin and high-spin upon irradiation with two different wavelengths.

    • Sreejith Shankar
    • , Morten Peters
    •  & Rainer Herges

  • Article
    | Open Access

    Myoglobin bound to carbon monoxide undergoes an ultrafast light-induced reaction, which ends up in a photolyzed carbon monoxide and a spin transition of the iron center. Here, the authors employ quantum wavepacket dynamics to show that photolysis precedes the spin transition, a mechanism dominated by strong electron-nuclear couplings.

    • Konstantin Falahati
    • , Hiroyuki Tamura
    •  & Miquel Huix-Rotllant

  • Article
    | Open Access

    Methane- and ammonia-oxidizing bacteria use the integral membrane, copper-dependent enzymes particulate methane monooxygenase (pMMO) and ammonia monooxygenase (AMO) to oxidize methane and ammonia. Here the authors structurally characterize the copper-binding protein PmoD, which contains an unusual CuA site and their genetic analyses strongly support a pMMO and AMO related function of PmoD.

    • Oriana S. Fisher
    • , Grace E. Kenney
    •  & Amy C. Rosenzweig

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