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Showing 1–4 of 4 results
Advanced filters: Author: Thomas Spatzal Clear advanced filters

  • The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is a large metal cluster with an important role in biological nitrogen fixation. Here, the authors use spatially resolved refinement of the anomalous scattering contributions of the iron atoms to determine the resting-state electron distribution of FeMoco.

    • Thomas Spatzal
    • Julia Schlesier
    • Oliver Einsle
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-7

  • The molybdenum cofactor (Moco) is found in the active site of numerous enzymes, but the mechanism of molybdate insertion is not clear. Now, the mechanism of the final maturation step, in which adenylated molybdopterin and molybdate are the substrates, has been revealed. X-ray crystallography of an Mo-insertase identified adenylated Moco as an unexpected intermediate in this reaction sequence.

    • Corinna Probst
    • Jing Yang
    • Tobias Kruse
    Research
    Nature Chemistry
    Volume: 13, P: 758-765

  • It can be challenging to obtain meaningful and accurate structural information for air-sensitive proteins. This protocol describes the application of customized vacuum manifold and anaerobic chamber setups for the purification and cryo-electron microscopy analysis of air-sensitive nitrogenase enzymes.

    • Rebeccah A. Warmack
    • Belinda B. Wenke
    • Douglas C. Rees
    Protocols
    Nature Protocols
    Volume: 19, P: 2026-2051