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Showing 1–10 of 10 results
Advanced filters: Author: Serena DeBeer Clear advanced filters
  • Copper-containing proteins can be classified into types 1 and 2, depending on their functional or spectroscopic properties. Now, a protein that fits neither type has been built using a scaffold made from the protein Pseudomonas aeruginosa azurin.

    • Kyle M. Lancaster
    • Serena DeBeer George
    • Harry B. Gray
    Research
    Nature Chemistry
    Volume: 1, P: 711-715
  • Complexes of iron in high oxidation states play a pivotal role as active intermediates in numerous catalytic processes. Now, using a multimethod approach on a single molecular system, it has been shown that a stable high-valent Fe(VI) nitride can be converted to a reactive, superoxidized, heptavalent Fe(VII) nitride.

    • Martin Keilwerth
    • Weiqing Mao
    • Karsten Meyer
    ResearchOpen Access
    Nature Chemistry
    Volume: 16, P: 514-520
  • Due to their stability, reduction of amides typically requires harsh conditions or strong reductants. Here the authors report a method for amide reduction with molecular hydrogen under mild conditions by use of magnetocatalysis.

    • Sheng-Hsiang Lin
    • Sihana Ahmedi
    • Alexis Bordet
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13
  • X-ray spectroscopy offers element-selective probes of diverse (bio)chemical systems. Close coupling of experiment with ab initio calculations unveils the rich electronic structural information available and facilitates practical, chemical interpretation of spectra, as discussed in this Review.

    • Zachary Mathe
    • Dimitrios Maganas
    • Serena DeBeer
    Reviews
    Nature Reviews Chemistry
    Volume: 9, P: 436-453
  • By obtaining structural snapshots of the catalytic cycle of NADH:quinone oxidoreductase from Vibrio cholerae, the authors uncover its mechanism. They show how electrons are shuttled and determine the importance of the [2Fe-2S] cluster in the movement of the electron transfer switch.

    • Jann-Louis Hau
    • Susann Kaltwasser
    • Günter Fritz
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1686-1694
  • The multistep incorporation process of the catalytic NiFe(CN)2(CO) cofactor into [NiFe]-hydrogenase was deciphered by isolating key maturation intermediates, which were characterized by biochemical and a variety of spectroscopic techniques.

    • Giorgio Caserta
    • Sven Hartmann
    • Oliver Lenz
    Research
    Nature Chemical Biology
    Volume: 19, P: 498-506
  • Inexpensive iron catalysts often exhibit low activity in ammonia decomposition due to a strong iron-nitrogen binding energy. Here the authors demonstrate that combining iron with cobalt to form a Fe-Co bimetallic catalyst overcomes this limitation, presenting a promising solution for enhancing ammonia decomposition efficiency.

    • Shilong Chen
    • Jelena Jelic
    • Malte Behrens
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-11
  • Despite extensive investigations of mixed-valence complexes, molecules with intermediate spin states have remained elusive. Now, selenium- and tellurium-bridged mixed-valent iron dimers have been prepared in which a balance of Heisenberg exchange and double-exchange coupling of the unpaired electron, combined with moderate vibronic contributions, stabilizes S = 3/2 ground spin states.

    • Justin T. Henthorn
    • George E. Cutsail III
    • Serena DeBeer
    ResearchOpen Access
    Nature Chemistry
    Volume: 14, P: 328-333
  • The four-coordinate iron sites of typical iron–sulfur clusters rarely react with small molecules, implicating three-coordinate iron in many catalytic cycles. Now, a [4Fe-3S] cluster featuring three-coordinate iron sulfide that resembles the proposed substrate binding site has been synthesized. This cluster shows biomimetic reactivity with a low-spin electronic configuration.

    • Daniel E. DeRosha
    • Vijay G. Chilkuri
    • Patrick L. Holland
    Research
    Nature Chemistry
    Volume: 11, P: 1019-1025