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Showing 1–13 of 13 results
Advanced filters: Author: Christophe Léger Clear advanced filters

  • FeFe hydrogenases are highly efficient H2 producing enzymes; however, they can be inactivated by O2. Now, a mechanism for O2 diffusion within FeFe hydrogenases and its reactions at the active site of the enzyme has been proposed. These findings could help with the design of hydrogenase mutants with increased resistance to oxidative damage.

    • Adam Kubas
    • Christophe Orain
    • Christophe Léger
    Research
    Nature Chemistry
    Volume: 9, P: 88-95

  • [FeFe]-hydrogenases catalyze the conversion of protons and electrons to molecular hydrogen, but upon exposure to oxygen, their catalytic cofactor is irreversibly inactivated. Here, the authors determine the crystal structure of hydrogenase CbA5H and identify a cysteine residue, which acts as a safety cap that shields the active site from oxygen.

    • Martin Winkler
    • Jifu Duan
    • Thomas Happe
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10

  • Biotechnological applications of hydrogenases are limited by their susceptibility to inactivation by oxygen, thought to proceed by trapping a reduced O2 in the active site. Electrochemical and spectroscopic studies using various electron acceptors now show that oxygen inactivation is not linked to oxygen atom donation.

    • Abbas Abou Hamdan
    • Bénédicte Burlat
    • Sébastien Dementin
    Research
    Nature Chemical Biology
    Volume: 9, P: 15-17

  • Oxygen sensitivity hampers applications of metal-dependent CO2 reductases. Here, Oliveira et al. describe how an allosteric disulfide bond controls the activity of a CO2 reductase, preventing its physiological reduction during transient O2 exposure and allowing aerobic handling of the enzyme.

    • Ana Rita Oliveira
    • Cristiano Mota
    • Inês A. Cardoso Pereira
    Research
    Nature Chemical Biology
    Volume: 20, P: 111-119

  • Integration of biocatalysts into redox films has systematically led to a loss of their intrinsic reversibility. Now, a specially designed redox hydrogel preserves the reversibility of a [FeFe] hydrogenase and the importance of this feature for energy conversion applications is demonstrated.

    • Steffen Hardt
    • Stefanie Stapf
    • Nicolas Plumeré
    Research
    Nature Catalysis
    Volume: 4, P: 251-258

  • FeFe hydrogenases, the enzymes that oxidize or produce H2, are inactivated under oxidizing conditions. Here, it is shown that this inactivation results from H2 binding to coordination positions that are normally blocked by intrinsic CO ligands. This flexibility of the active site prevents irreversible oxidative damage.

    • Vincent Fourmond
    • Claudio Greco
    • Christophe Léger
    Research
    Nature Chemistry
    Volume: 6, P: 336-342

  • Comparing the Michaelis constants and rates of inhibition of wild-type and mutant hydrogenases reveals the quantitative impact of amino acid changes on the diffusion rates of H2, CO and O2 and suggests design strategies for creating oxygen-tolerant hydrogenases.

    • Pierre-Pol Liebgott
    • Fanny Leroux
    • Christophe Léger
    Research
    Nature Chemical Biology
    Volume: 6, P: 63-70

  • Understanding the relationship between reaction rate and thermodynamic driving force is central to developing efficient catalysts. This Perspective describes this relationship and the conditions that can give rise to reversible catalysis, which is relevant to energy conversions of fuels and motor proteins alike.

    • Vincent Fourmond
    • Nicolas Plumeré
    • Christophe Léger
    Reviews
    Nature Reviews Chemistry
    Volume: 5, P: 348-360