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Showing 1–3 of 3 results
Advanced filters: Author: Jae-Hun Jeoung 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

  • The CO dehydrogenase–acetyl-coenzyme A synthase complex produces acetyl-coenzyme A from CO2, but its structural dynamics during catalysis remain unresolved. Now cryo-EM maps of six intermediate states reveal how ligand binding to a Ni–Fe cluster orchestrates the conformational changes of the complex during catalysis.

    • Jakob Ruickoldt
    • Julian Kreibich
    • Petra Wendler
    ResearchOpen Access
    Nature Catalysis
    Volume: 8, P: 657-667

  • Some biological reactions can require thermodynamically unfavourable electron transfer processes, the occurrence of which are not yet fully understood. Here, the authors provide the structural basis of energy transduction during the reductive activation of B12-dependent methyltransferases.

    • Sandra E. Hennig
    • Sebastian Goetzl
    • Holger Dobbek
    Research
    Nature Communications
    Volume: 5, P: 1-7