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Showing 1–2 of 2 results
Advanced filters: Author: Nathaniel S. Sickerman Clear advanced filters

  • The M-cluster in the active site of nitrogenase is derived from an 8Fe core assembled via coupling and rearrangement of two [Fe4S4] clusters concomitant with the insertion of an interstitial carbon and a ninth sulfur. Now, by combining synthetic [Fe4S4] clusters and assembly with a protein template, it has been shown that sulfite gives rise to the ninth sulfur that is inserted into the nitrogenase cofactor after the radical SAM-dependent carbide insertion and cofactor core rearrangement.

    • Kazuki Tanifuji
    • Chi Chung Lee
    • Markus W. Ribbe
    Research
    Nature Chemistry
    Volume: 10, P: 568-572

  • The Fe protein of nitrogenase contains a redox-active [Fe4S4] cluster that plays a key role in electron transfer and substrate reduction. Here, Hu and co-workers show that the Fe protein of Methanosarcina acetivorans can reduce CO2 and CO to hydrocarbons under ambient conditions.

    • Martin T. Stiebritz
    • Caleb J. Hiller
    • Yilin Hu
    Research
    Nature Catalysis
    Volume: 1, P: 444-451