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Showing 1–3 of 3 results
Advanced filters: Author: Christian Teutloff Clear advanced filters

  • The mechanism by which the [NiFe4S4] cluster of carbon monoxide dehydrogenases (CODHs) catalyses CO2 reduction is poorly understood. Now the structures of all catalytically relevant states of a CODH are solved, revealing the dynamics of the cluster during turnover and the role of Ni in CO2 activation.

    • Yudhajeet Basak
    • Christian Lorent
    • Holger Dobbek
    ResearchOpen Access
    Nature Catalysis
    Volume: 8, P: 794-803

  • Rhodobacter capsulatus NAD+ dependent formate dehydrogenase (RcFDH) is a molybdoenzyme that catalyses the reversible oxidation of formate to carbon dioxide, and is of interest for biotechnological applications. Here the authors present the cryo-EM structures of RcFDH as isolated from R. capsulatus and in the reduced state with bound NADH, and discuss the enzyme mechanism.

    • Christin Radon
    • Gerd Mittelstädt
    • Petra Wendler
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-9

  • Certain oxygen-tolerant hydrogenases contain a unique [4Fe-3S] cluster near the catalytic site, but the role of this cofactor is not fully understood. Crystallographic, spectroscopic and computational data now provide evidence for redox-dependent transformations of this cluster, potentially explaining how specialized hydrogenases can safely reduce inhibitory O2.

    • Stefan Frielingsdorf
    • Johannes Fritsch
    • Patrick Scheerer
    Research
    Nature Chemical Biology
    Volume: 10, P: 378-385