Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–5 of 5 results
Advanced filters: Author: Martin T. Stiebritz Clear advanced filters

  • 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

  • The iron protein components of bacterial nitrogenases are capable of reducing carbon dioxide (CO2) to carbon monoxide (CO) in the absence of their catalytic partners, mimicking the activity of CO dehydrogenase.

    • Johannes G Rebelein
    • Martin T Stiebritz
    • Yilin Hu
    Research
    Nature Chemical Biology
    Volume: 13, P: 147-149

  • A recently proposed structure of an N2-bound Mo-nitrogenase has sparked considerable attention, although the direct evidence for N2 binding and sulfur mobilization during turnover has remained elusive. Now, additional spectroscopic and kinetic measurements further support this state and provide evidence that belt-sulfur displacement is an essential aspect of the nitrogenase mechanism.

    • Chi Chung Lee
    • Wonchull Kang
    • Yilin Hu
    Research
    Nature Catalysis
    Volume: 5, P: 443-454

  • Located in the catalytically important belt region, the ‘ninth sulfur’ of the nitrogenase cofactor has now been shown to be inserted through coordination of sulfite by two cluster iron atoms at a vacant belt site. This is followed by in situ reduction of sulfite to sulfide, which enables the subsequent transfer and functionalization of the cofactor.

    • Kazuki Tanifuji
    • Andrew J. Jasniewski
    • Markus W. Ribbe
    Research
    Nature Chemistry
    Volume: 13, P: 1228-1234

  • NifB is a key enzyme in the biosynthesis pathway of the nitrogenase FeMo cofactor. Here, the authors investigate the maturation of its iron-sulfur clusters by EPR and biochemical analyses, showing how individual precursor clusters participate in the formation of the final iron-sulfur cluster.

    • Lee A. Rettberg
    • Jarett Wilcoxen
    • Yilin Hu
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-8