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Showing 1–4 of 4 results
Advanced filters: Author: Louis Noodleman Clear advanced filters

  • Iron–sulfur metalloproteins are critical for electron transfer in bacterial metabolism, but most crystal structures are insufficient for their in-depth study. Now, acquisition of an iron–sulfur protein structure at ultra-high resolution enables detailed visualization of its electron distribution.

    • Louis Noodleman
    News & Views
    Nature Chemical Biology
    Volume: 12, P: 391-392

  • Analysis of the thermodynamics of protein–N-glycan interactions perturbed by mutations has revealed an enthalpy–entropy compensation that depends on the electronics of the interacting side chains. Machine-learned and statistical models showed that protein–N-glycan interactions highly correlate with stereoelectronic effects, and that a major part of protein–N-glycan interactions can be explained using the energetic rules of frontier molecular orbital interactions.

    • Maziar S. Ardejani
    • Louis Noodleman
    • Jeffery W. Kelly
    Research
    Nature Chemistry
    Volume: 13, P: 480-487

  • Iron–sulfur metalloproteins are widespread and efficient catalysts for multielectron reduction of small molecules. Now, research shows that simple Fe4S4 cofactors and related complexes can perform effective reductive chemistry producing small hydrocarbons from CO2 and CO.

    • Louis Noodleman
    News & Views
    Nature Catalysis
    Volume: 1, P: 383-384