126 results found
    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.
    1. Biochemistry and Chemical Biology
    2. Cancer Biology

    Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins

    Marta A Uzarska, Veronica Nasta ... Roland Lill
    Cell biological, biochemical and structural studies reveal the mechanistic roles of two new mitochondrial iron-sulfur protein assembly factors, explaining the patho-biochemical defects of affected patients.
    1. Biochemistry and Chemical Biology

    The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis

    Jonathan G Van Vranken, Mi-Young Jeong ... Jared Rutter
    The essential function of ACP is not related to mitochondrial fatty acid and lipoic acid synthesis, but rather an evolutionarily-conserved role in iron sulfur cluster biogenesis.
    1. Biochemistry and Chemical Biology
    2. Microbiology and Infectious Disease

    Cellular assays identify barriers impeding iron-sulfur enzyme activity in a non-native prokaryotic host

    Francesca D'Angelo, Elena Fernández-Fueyo ... Gregory Bokinsky
    The intracellular network that distributes iron-sulfur clusters in bacteria is surprisingly 'plug and play' with iron-sulfur enzymes acquired from distantly related species, whereas the intracellular electron transfer network often needs plug adapters to connect with foreign enzymes.
    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

    Metal Biology: Bridging a gap in iron-sulfur cluster assembly

    Erin L. McCarthy, Squire J. Booker
    Insight
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    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
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    1. Structural Biology and Molecular Biophysics

    Functional asymmetry and electron flow in the bovine respirasome

    Joana S Sousa, Deryck J Mills ... Werner Kühlbrandt
    Cryo-EM structure of the mammalian respiratory supercomplex containing complexes I, III and IV shows a functional asymmetry of complex III, providing strong evidence for directed electron flow in the respirasome.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase

    Chris Furlan, Nipa Chongdar ... James A Birrell
    Cryo-EM and particle classification techniques reveal how the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima multimerizes to connect distant active sites and reveal different conformational states that enable catalysis.
    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
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