Biocatalysis articles within Nature Communications

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  • Article
    | Open Access

    The biosynthetic pathway of preakuammicine, a monoterpene precursor of the anti-cancer agent vinblastine, has remained largely unexplored. Here, the authors provide transcriptomic and biochemical data to identify two enzymes that, in tandem, convert strictosidine to akuammicine, the stable shunt product of preakuammicine.

    • Evangelos C. Tatsis
    • , Inês Carqueijeiro
    •  & Sarah E. O’Connor

  • Article
    | Open Access

    Coupling synthetic biology and chemical reactions in cells is a challenging task. The authors engineer bacteria capable of generating bromo-metabolites, develop a mild Suzuki-Miyaura cross-coupling reaction compatible with cell growth and carry out the cross-coupling chemistry in live cell cultures.

    • Sunil V. Sharma
    • , Xiaoxue Tong
    •  & Rebecca J. M. Goss

  • Article
    | Open Access

    The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable amino acid mutation can lead to substantial Kemp eliminase activity.

    • Valeria A. Risso
    • , Sergio Martinez-Rodriguez
    •  & Jose M. Sanchez-Ruiz

  • Article
    | Open Access

    Palladium (Pd) is a well-known catalyst in organic chemistry but its use in nanomedicine is limited. Here, the authors design a Pd nanoparticle that triggers the activation of an antitumour prodrugin vivo, which shows efficacy and improves toxicity compared to traditional solvent- and nanoparticle-drug formulations.

    • Miles A. Miller
    • , Bjorn Askevold
    •  & Ralph Weissleder

  • Article
    | Open Access

    Systematically understanding the sequence determinants to substrate specificity for enzymes has implications in areas from evolutionary biology to biocatalysis. Here, Whitehead and colleagues generate and analyse near-comprehensive single-mutation fitness landscapes for an amidase with three different substrates.

    • Emily E. Wrenbeck
    • , Laura R. Azouz
    •  & Timothy A. Whitehead

  • Article
    | Open Access

    The majority of enzymatic Kemp elimination reactions proceed via a well-established acid-base mechanism. Here, the authors show that cytochrome P450 is able to metabolize the leflunomide drug via a redox Kemp elimination, offering new insights into enzyme catalysis.

    • Aitao Li
    • , Binju Wang
    •  & Manfred T. Reetz

  • Article
    | Open Access

    Nitrogenases reduce inorganic nitrogen to organic ammonia in a crucial step of the nitrogen cycle. Here the authors show that the vanadium-nitrogenase ofAzotobacter vinelandii can also catalyse the in vivoconversion of carbon monoxide to hydrocarbons in a secondary non-biosynthetic pathway.

    • Johannes G. Rebelein
    • , Chi Chung Lee
    •  & Markus W. Ribbe

  • Article
    | Open Access

    The introduction of fluorine into organic molecules often requires prefunctionalised molecules or protection of reactive functional groups. Here, the authors report a biocatalytic method for the trifluoromethylation of unprotected phenols under mild conditions.

    • Robert C. Simon
    • , Eduardo Busto
    •  & Wolfgang Kroutil

  • Article
    | Open Access

    Natural biomolecules including heme-like porphyrins can be applied as sustainable chemical catalysts in lithium-oxygen batteries. Here, the authors show that the heme molecule can function as a soluble redox catalyst and oxygen shuttle for efficient oxygen evolution in non-aqueous lithium-oxygen cells.

    • Won-Hee Ryu
    • , Forrest S. Gittleson
    •  & André D. Taylor

  • Article
    | Open Access

    Diterpenes are plant products with high antioxidant properties and potential application as food additives and therapeutics. Here, the authors describe the complete biosynthetic pathway of carnosic acid and reconstruct it in yeast, opening the way to metabolic engineering of phenolic diterpenes.

    • Ulschan Scheler
    • , Wolfgang Brandt
    •  & Alain Tissier

  • Article
    | Open Access

    Building multi-component enzymatic processes in one pot is challenged by the inherent complexity of each biochemical system. Here, the authors use online mass spectroscopy and engineering systems theory to achieve forward design of a ten-membered reaction cascade.

    • Christoph Hold
    • , Sonja Billerbeck
    •  & Sven Panke

  • Article
    | Open Access

    While reversal of lysine methylation on histone tails is a well-established mechanism to tune gene expression, the existence of a similar arginine demethylation process is controversial. Here, the authors show that some jumonji enzymes possess both lysine and arginine demethylase activity in vitro.

    • Louise J. Walport
    • , Richard J. Hopkinson
    •  & Christopher J. Schofield

  • Article
    | Open Access

    There is a need for small-scale reactors that convert methane emissions to more valuable products to reduce climate impacts. Here, the authors show that printing 3D structures of the pMMO enzyme enables continuous methane conversion under ambient conditions and reduces mass transfer limitations.

    • Craig D. Blanchette
    • , Jennifer M. Knipe
    •  & Sarah E. Baker

  • Article
    | Open Access

    Designing catalysts and understanding the influence of ligands for particular transformations remains a highly challenging task. Here, the authors show that bisphosphine ligands can alter the geometry of the active site in silver catalysts, driving protonation and ultimately extrusion of carbon dioxide from formic acid.

    • Athanasios Zavras
    • , George N. Khairallah
    •  & Richard A. J. O’Hair

  • Article
    | Open Access

    Xanthones are pharmacologically and biosynthetically intriguing compounds. Here, the authors identify two cytochrome P450 enzymes, which hydroxylate and cyclize the benzophenone precursor to either 1,3,7- or 1,3,5-trihydroxyxanthones, and pinpoint residues that determine the alternative regioselectivities.

    • Islam El-Awaad
    • , Marco Bocola
    •  & Ludger Beerhues

  • Article
    | Open Access

    Early cells likely consisted of fatty acid vesicles enclosing magnesium-dependent ribozymes. Here, the authors show that fatty acid derivatives can form vesicles that, unlike those formed from only unmodified fatty acids, are stable in the presence of magnesium and could support ribozyme catalysis.

    • Katarzyna P. Adamala
    • , Aaron E. Engelhart
    •  & Jack W. Szostak

  • Article
    | Open Access

    The proteasome, an essential molecular machine, is a threonine protease, but the evolution and the components of its proteolytic centre are unclear. Here, the authors use structural biology and biochemistry to investigate the role of proteasome active site residues on maturation and activity.

    • Eva M. Huber
    • , Wolfgang Heinemeyer
    •  & Michael Groll

  • Article
    | Open Access

    DNA hybridisation thermodynamics parameters underlie rational design of oligonucleotides for diagnostics and nanotechnology. Here, the authors present an accurate method to measure the free energy of a given DNA structure at specific temperature and buffer conditions.

    • Chunyan Wang
    • , Jin H. Bae
    •  & David Yu Zhang

  • Article
    | Open Access

    Auxilliary Activity Family 5 (AA5) comprises mononuclear copper radical oxidases with catalytic diversity that is not well characterised. Here, structural, phylogenetic and biochemical analyses advance our understanding of the potential biological and biotechnology functions of these proteins.

    • DeLu (Tyler) Yin
    • , Saioa Urresti
    •  & Harry Brumer

  • Article
    | Open Access

    Environmental DNA from unculturable microorganisms contains genes with useful functions that remain difficult to identify and isolate. Here Colin, Kintses et al.demonstrate the screening of millions of samples in pL volumes to directly identify new enzymatic activities and complements sequence-based approaches.

    • Pierre-Yves Colin
    • , Balint Kintses
    •  & Florian Hollfelder

  • Article
    | Open Access

    A major challenge in following electron transfer through dithiol/disulfide exchange is the dearth of accompanying spectroscopic effects. Here, the authors use single-molecule Förster resonance energy transfer experiments to illuminate disulfide bond rearrangements within the enzyme quiescin sulfhydryl oxidase.

    • Iris Grossman
    • , Haim Yuval Aviram
    •  & Deborah Fass

  • Article
    | Open Access

    Cobalamin-dependent radical SAM enzymes are proposed as methyltransferases in many biosynthetic pathways. Here, the authors study a pathway involving the methylation of tryptophan, showing that methylcob(III)alamin is the most likely cofactor and propose a radical-based C-methylation mechanism.

    • Alhosna Benjdia
    • , Stéphane Pierre
    •  & Olivier Berteau

  • Article
    | Open Access

    Artificial metalloenzymes (ArMs) have the potential to improve transition metal reactivity in complex media. Here, the authors link a dirhodium catalyst to a prolyl oligopeptidase to create an ArM that catalyzes enantioselective olefin cyclopropanation in aqueous solution.

    • Poonam Srivastava
    • , Hao Yang
    •  & Jared C. Lewis

  • Article
    | Open Access

    Copper-exchanged zeolites with mordenite structure can mimic the active sites in particulate methane monooxygenase. Here, the authors show that mordenite micropores can stabilize trinuclear copper-oxo clusters that exhibit a high reactivity towards activation of carbon–hydrogen bonds in methane.

    • Sebastian Grundner
    • , Monica A.C. Markovits
    •  & Johannes A. Lercher

  • Article
    | Open Access

    Most radical SAM enzymes use a [4Fe-4S] cluster to generate a 5′-deoxyadenosyl radical. Here the authors show the radical SAM thiamin pyrimidine synthase ThiC comprises an additional active site metal, probably representing an evolutionary link between the radical SAM and adenosylcobalamin-dependent enzyme superfamilies.

    • Michael K. Fenwick
    • , Angad P. Mehta
    •  & Steven E. Ealick

  • Article
    | Open Access

    Organometallic complexes are effective hydrogenation catalysts for organic reactions. Here the authors report for the first time that transfer hydrogenation catalysis can take place inside the cell and could be used as a novel anticancer strategy.

    • Joan J. Soldevila-Barreda
    • , Isolda Romero-Canelón
    •  & Peter J. Sadler

  • Article |

    The Achmatowicz reaction involves the conversion of furans into dihydropyrans, classically with the use of bromine. Here, the authors couple an enzymatic oxygen activation with a chloroperoxidase-mediated oxygen transfer, providing a biocatalytic route to a formal Achmatowicz reaction.

    • Daniel Thiel
    • , Diana Doknić
    •  & Jan Deska

  • Article |

    The transfer of a phosphate group from a CDP-linked donor to an acceptor alcohol is catalysed by CDP-alcohol phosphotransferases. Here, Sciara et al. report crystal structures of a CDP-alcohol phosphotransferase, define roles of conserved residues and propose a mechanism of action for this protein family.

    • Giuliano Sciara
    • , Oliver B. Clarke
    •  & Filippo Mancia

  • Article |

    The enzyme butyrylcholinesterase (BChE) can metabolize cocaine, albeit at relatively low speeds. Here the authors use computational methods to define mutations that increase BChE-mediated cocaine hydrolysis, achieving a catalytic activity comparable to that of one of the fastest naturally occurring enzyme.

    • Fang Zheng
    • , Liu Xue
    •  & Chang-Guo Zhan

  • Article |

    Enzymes have been considered as biocatalysts for organic chemistry, however their broad application has been somewhat hampered by the requirement for reducing cofactors. Here, the authors demonstrate that, in the presence of titania photocatalysts, water can be used as the sacrificial electron donor.

    • Maria Mifsud
    • , Serena Gargiulo
    •  & Avelino Corma

  • Article |

    Methane is a promising renewable carbon source for chemical synthesis, yet methane bio-gas is currently underutilised as a feedstock. Here the authors examine the metabolic processes of methanotrophic bacteria to assess their use for conversion of methane to value-added chemical products.

    • M. G. Kalyuzhnaya
    • , S. Yang
    •  & M. E. Lidstrom

  • Review Article |

    High-valent iron–oxo and –nitrido complexes are intermediates in the catalytic cycles of various metalloenzymes that activate dioxygen and dinitrogen. Hohenbergeret al. review the advances in the chemistry of model high-valent iron–oxo and –nitrido systems and relate them to our understanding of related enzymes.

    • Johannes Hohenberger
    • , Kallol Ray
    •  & Karsten Meyer

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