Global ETD Search
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Showing 1 to 4 of 4 for “"Mo-nitrogenase"”.
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Site-selective Labeling of the Nitrogenase Iron-Molybdenum Cofactor
Nitrogenases are enzymes known to catalyze the kinetically challenging, and biologically important, reduction of N₂ to NH₃. The mechanism of these enzymes, and in particular, the chemistry that occurs at the catalytic cofactor of the Mo nitrogenase, the iron- molybdenum cofactor (FeMo-co), has been …
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Azotobacter vinelandii Nitrogenase: Multiple Substrate-Reduction Sites and Effects of pH on Substrate Reduction and CO Inhibition
Mo-nitrogenase consists of two component proteins, the Fe protein and the MoFe protein. The site of substrate binding and reduction within the Mo-nitrogenase is provided by a metallocluster, the FeMo cofactor, located in the a-subunit of the MoFe protein. The FeMo cofactor's polypeptide environment …
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Early evolution of environments and metabolism: insights from nitrogen, selenium and sulfur isotopes
… We conclude that the origin of life can be more plausibly explained if the various building blocks of living cells slowly emerged from global geochemical cycles. In the second part of my thesis (Chapters 2-3), I explore how microorganisms exploited and modified these cycles, in particular …
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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. …