7 results found
    1. Biochemistry and Chemical Biology
    2. Evolutionary Biology

    Nitrogenase resurrection and the evolution of a singular enzymatic mechanism

    Amanda K Garcia, Derek F Harris ... Betül Kaçar
    Life is constrained in its sampling of protein sequence space to catalyze one of the most energetically challenging biochemical reactions.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor

    Thomas Spatzal, Kathryn A Perez ... Douglas C Rees
    Unanticipated rearrangements in the nitrogenase active site establish the dynamic nature of the FeMo-cofactor during catalysis.
    Short Report Updated
    Formats available:
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    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster

    Trixia M Buscagan, Jens T Kaiser, Douglas C Rees
    X-ray crystal structures capture ATP-dependent chalcogenide exchange from selenocyanate at the nitrogenase Fe protein cluster in the absence of the MoFe protein, an unexpected result as the Fe protein cluster is not traditionally perceived as a site of substrate binding.
    Short Report Updated
    Formats available:
    • HTML
    • PDF
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Nitrogen Fixation: Waltzing around cofactors

    Percival Yang-Ting Chen, Elizabeth C Wittenborn, Catherine L Drennan
    Insight
    Formats available:
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    1. Computational and Systems Biology
    2. Physics of Living Systems

    Defining hierarchical protein interaction networks from spectral analysis of bacterial proteomes

    Mark A Zaydman, Alexander S Little ... Arjun S Raman
    The emergent organization of bacterial proteomes—the integration of proteins into collective networks that encode function—can be defined purely from spectral analysis of ortholog covariation across extant diversity.
    1. Biochemistry and Chemical Biology

    Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients

    Andrew Melber, Un Na ... Dennis R Winge
    Mitochondrial proteins Nfu1 and BolA3 mediate the transfer of preformed [4Fe-4S] clusters within the mitochondria to recipient proteins to shield clusters from oxidative damage during transfer.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC protein Rli1 for iron-sulfur cluster insertion

    Viktoria Désirée Paul, Ulrich Mühlenhoff ... Roland Lill
    Two newly identified assembly factors for the ribosome-associated iron-sulfur protein Rli1 reveal a general mechanism for how the cytosolic iron-sulfur protein assembly (CIA) machinery recruits apoproteins.

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