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Showing 1–4 of 4 results
Advanced filters: Author: Julian Esselborn Clear advanced filters

  • In cells, di-iron hydrogenases require three maturases to facilitate proper assembly of metal clusters. Reconstitution experiments with synthetic cofactor mimics coupled with functional and spectroscopic characterization now show these helper proteins are not needed in vitro to form highly active H2-producing catalysts.

    • Julian Esselborn
    • Camilla Lambertz
    • Thomas Happe
    Research
    Nature Chemical Biology
    Volume: 9, P: 607-609

  • An inorganic chemical approach to biomolecular design is used to generate ‘cages’ that can simultaneously promote symmetry and multiple modes of protein interactions.

    • Eyal Golub
    • Rohit H. Subramanian
    • F. Akif Tezcan
    Research
    Nature
    Volume: 578, P: 172-176

  • Of the four intermediates in the catalytic cycle of [FeFe]-hydrogenases, the hydride state still has eluded characterization. Here, the authors shift the reaction equilibrium for three hydrogenases and enrich the hydride-bound species, characterizing them using a real-time IR spectroscopic technique.

    • Martin Winkler
    • Moritz Senger
    • Thomas Happe
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-7

  • [FeFe]-hydrogenases catalyze H2-evolution and -oxidation at very high turnover-rates. Here the authors provide experimental evidence for the proposed proton-transfer (PT) pathway by kinetically, spectroscopically, and crystallographically characterizing eleven mutants from the two [FeFe]-hydrogenases CpI and HydA1.

    • Jifu Duan
    • Moritz Senger
    • Martin Winkler
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11