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Showing 1–7 of 7 results
Advanced filters: Author: Sven T. Stripp Clear advanced filters

  • Structural and biochemical studies of the Mycobacterium smegmatis hydrogenase Huc provides insights into how [NiFe] hydrogenases oxidize trace amounts of atmospheric hydrogen and transfer the electrons liberated via quinone transport.

    • Rhys Grinter
    • Ashleigh Kropp
    • Chris Greening
    ResearchOpen Access
    Nature
    Volume: 615, P: 541-547

  • Understanding metalloenzymes can inspire the design of molecular catalysts. Employing signal-enhanced nuclear magnetic resonance spectroscopy on parahydrogen-reduced [Fe]-hydrogenase, two reaction intermediates have been characterized. This work paves the way toward a microscopic understanding of these metalloenzymes.

    • Sven T. Stripp
    News & Views
    Nature Catalysis
    Volume: 7, P: 1264-1265

  • 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

  • The structure and function of the MCR activation complex from Methanococcus maripaludis were revealed, demonstrating its ATP-dependent ability to activate MCR and form methane while uncovering a unique electron transfer pathway involving iron–sulfur clusters similar to the nitrogenase cofactor intermediates.

    • Fidel Ramírez-Amador
    • Sophia Paul
    • Jan Michael Schuller
    ResearchOpen Access
    Nature
    Volume: 642, P: 814-821

  • A landmark vibrational study from 15 years ago established much of what we know about hydrogenase mechanisms

    • Sven T. Stripp
    News & Views
    Nature Reviews Chemistry
    Volume: 5, P: 146-147

  • Acetogenic bacteria deploy electron-bifurcating transhydrogenase for electron carrier adjustments in the ancient Wood-Ljungdahl pathway. Here, the authors report a cryo-EM structure of the Stn class transhydrogenase from the Sporomusa ovata and dissect its electron transfer pathway.

    • Anuj Kumar
    • Florian Kremp
    • Jan M. Schuller
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • [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