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Showing 1 to 10 of 10 for “"FeMo-cofactor"”.

  1. Spectroscopic investigation of nitrogenase: EPR and MCD studies of the FeMo cofactor and the P-cluster

    … from different binding of the substrate to the cofactor (side-on or terminal binding) or the difference of the substrate binding to either Fe or Mo of the cofactor. Parallel studies were performed on a variant MoFe protein, alpha-195<sup>Gln</sup>, which exhibited different signals from the …

    lsu-thes Repository record for Spectroscopic investigation of nitrogenase: EPR and MCD studies of the FeMo cofactor and the P-cluster (opens in a new tab)

  2. Biosynthesis of the Nitrogenase FeMo-cofactor from Azotobacter vinelandii: Involvement of the NifEN complex, NifX and the Fe protein

    The iron-molybdenum cofactor (FeMo-cofactor) of nitrogenase is the subject of one the most intensive biochemical/genetic detective cases of modern science. At the active site of nitrogenase, the FeMo-cofactor not only represents the heart of biological nitrogen fixation, but its synthesis also …

    vt Repository record for Biosynthesis of the Nitrogenase FeMo-cofactor from Azotobacter vinelandii: Involvement of the NifEN complex, NifX and the Fe protein (opens in a new tab)

  3. The Biosynthesis and Function of Nitrogenase Metalloclusters

    … of the Fe protein, and the P-cluster [8Fe7S] and FeMo-cofactor [7Fe-9S-Mo-X-homocitrate], both contained within the MoFe protein. These metal-complexes play a vital role in enzyme activity during electron transport and substrate reduction. It is known that the FeMo-cofactor provides the site of …

    vt Repository record for The Biosynthesis and Function of Nitrogenase Metalloclusters (opens in a new tab)

  4. Azotobacter vinelandii nitrogenase: role of the MoFe protein α-subunit histidine-195 residue in catalysis

    … this histidine residue is associated with the FeMo-cofactor binding domain and probably provides an NH→S hydrogen bond to a central bridging sulfide located within FeMo-cofactor. The present study investigates the role of the α-histidine-195 residue in nitrogenase catalysis by examining the …

    vt Repository record for Azotobacter vinelandii nitrogenase: role of the MoFe protein α-subunit histidine-195 residue in catalysis (opens in a new tab)

  5. Roles of MoFe protein α-274-histidine, α-276-tyrosine and α-277-arginine residues in Azotobacter vinelandii nitrogenase catalysis

    … essential ligand to one of the Fe atoms on the FeMo-cofactor, and its substitutions resulted in inactive nitrogenase. In order to study the structural-functional relationship of the protein environment in this region with respect to the FeMo-cofactor, subtle changes were introduced through …

    vt Repository record for Roles of MoFe protein α-274-histidine, α-276-tyrosine and α-277-arginine residues in Azotobacter vinelandii nitrogenase catalysis (opens in a new tab)

  6. Genetic analysis of nifF and nifA and site-directed mutagenesis of nifE in Azotobacter vinelandii

    … transport), nifA (nif gene regulation) and nifE (FeMo-cofactor biosynthesis) genes from <i>Azotobacter vinelandii</i> were genetically analyzed. The nucleotide sequence of the nifF gene, which encodes a flavodoxin, was determined. Specific mutation strains indicated that in <i>A vinelandii</i> …

    vt Repository record for Genetic analysis of nifF and nifA and site-directed mutagenesis of nifE in Azotobacter vinelandii (opens in a new tab)

  7. Azotobacter vinelandii Nitrogenase: Multiple Substrate-Reduction Sites and Effects of pH on Substrate Reduction and CO Inhibition

    … is provided by a metallocluster, the FeMo cofactor, located in the a-subunit of the MoFe protein. The FeMo cofactor's polypeptide environment appears to be intimately involved in the delicate control of the MoFe protein's interactions with its substrates and inhibitors (Fisher K et …

    vt Repository record for Azotobacter vinelandii Nitrogenase: Multiple Substrate-Reduction Sites and Effects of pH on Substrate Reduction and CO Inhibition (opens in a new tab)

  8. Role of the MoFe Protein β-95-Cysteinyl Residue in Nitrogenase Catalysis in <i>Azotobacter vinelandii</i>

    … with substitutions at β-Cys contain typical FeMo cofactor EPR signal. The β-95<sup>Asp</sup> MoFe protein also has significant nitrogenase activity, but lower, suggesting that β-Cys is not absolutely required for both FeMo cofactor insertion and nitrogenase activity. In order to characterize …

    vt Repository record for Role of the MoFe Protein β-95-Cysteinyl Residue in Nitrogenase Catalysis in <i>Azotobacter vinelandii</i> (opens in a new tab)

  9. Azotobacter vinelandii Nitrogenase: Effect of Amino-Acid Substitutions at the Alpha Gln-191 Residue of the MoFe Protein on Substrate Reduction and CO Inhibition

    The FeMo cofactor is one of two types of prosthetic group found in the larger of the two nitrogenase component proteins, called the MoFe protein, and it is strongly implicated as the substrate binding and reduction site. The glutamine-191 residue in the Alpha-subunit of the MoFe protein of A. …

    vt Repository record for Azotobacter vinelandii Nitrogenase: Effect of Amino-Acid Substitutions at the Alpha Gln-191 Residue of the MoFe Protein on Substrate Reduction and CO Inhibition (opens in a new tab)

  10. Characterizing a structural and functional model of nitric oxide reductase performing NO and O2 reduction in engineered myoglobin

    … metal binding sites, such as those for the FeMo cofactor of nitrogenase, utilizing the Rosetta software suite are described in detail. Insights gained from the study of FeBMb and its relevance to NOR and HCO include evidence to support the so called trans mechanism of NO reduction, whereby 2 …

    uiuc Repository record for Characterizing a structural and functional model of nitric oxide reductase performing NO and O2 reduction in engineered myoglobin (opens in a new tab)