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The Fe protein, the dinitrogenase reductase or NifH, is a dimer of identical subunits which contains one [Fe 4 S 4] cluster and has a mass of approximately 60-64kDa. [2] The function of the Fe protein is to transfer electrons from a reducing agent, such as ferredoxin or flavodoxin to the nitrogenase protein.
FeMoco (FeMo cofactor) is the primary cofactor of nitrogenase. Nitrogenase is the enzyme that catalyzes the conversion of atmospheric nitrogen molecules N 2 into ammonia (NH 3) through the process known as nitrogen fixation. Because it contains iron and molybdenum, the cofactor is called FeMoco. Its stoichiometry is Fe 7 MoS 9 C.
Nitrogenase is thought to have evolved sometime between 1.5-2.2 billion years ago (Ga), [38] [39] although some isotopic support showing nitrogenase evolution as early as around 3.2 Ga. [40] Nitrogenase appears to have evolved from maturase-like proteins, although the function of the preceding protein is currently unknown. [41]
Vanadium nitrogenases are found in members of the bacterial genus Azotobacter as well as the species Rhodopseudomonas palustris and Anabaena variabilis. [1] [2] Most of the functions of vanadium nitrogenase match those of the more common molybdenum nitrogenases and serve as an alternative pathway for nitrogen fixation in molybdenum deficient conditions. [4]
It is thus suspected that Fe in a low-coordination environment is a key factor to the fixation of nitrogen by the nitrogenase enzyme, since its Fe–Mo cofactor also features Fe with low coordination numbers. [17] The average bond length of those bridging-end-on dinitrogen complexes is about 1.2 Å.
Abiological nitrogen fixation describes chemical processes that fix (react with) N 2, usually with the goal of generating ammonia. The dominant technology for abiological nitrogen fixation is the Haber process, which uses iron-based heterogeneous catalysts and H 2 to convert N 2 to NH 3. This article focuses on homogeneous (soluble) catalysts ...
Molecular binding occurs in biological complexes (e.g., between pairs or sets of proteins, or between a protein and a small molecule ligand it binds) and also in abiologic chemical systems, e.g. as in cases of coordination polymers and coordination networks such as metal-organic frameworks.
Its bonding is similar to that in nitrogen, but one extra electron is added to a π* antibonding orbital and thus the bond order has been reduced to approximately 2.5; hence dimerisation to O=N–N=O is unfavourable except below the boiling point (where the cis isomer is more stable) because it does not actually increase the total bond order ...