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Nitrogenase is an enzyme responsible for catalyzing nitrogen fixation, which is the reduction of nitrogen (N 2) to ammonia (NH 3) and a process vital to sustaining life on Earth. [9] There are three types of nitrogenase found in various nitrogen-fixing bacteria: molybdenum (Mo) nitrogenase, vanadium (V) nitrogenase, and iron-only (Fe ...
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]
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 ...
The dinitrogen complex trans-[IrCl(N 2)(PPh 3) 2] is made by treating Vaska's complex with aromatic acyl azides. It has a planar geometry. [7] The first preparation of a metal-dinitrogen complex using dinitrogen was reported in 1967 by Yamamoto and coworkers. They obtained [Co(H)(N 2)(PPh 3) 3] by reduction of Co(acac) 3 with AlEt 2 OEt under ...
In the solid state further bridging occurs between neighbours and when this compound is dissolved in hydrochloric acid a Re 3 Cl 12 3− complex forms. An example of a tetranuclear complex is hexadecamethoxytetratungsten W 4 (OCH 3) 12 with tungsten single bonds. A related group of clusters with the general formula M x Mo 6 X 8 such as PbMo 6 S 8.
The nitrogenase holoenzyme of A. vinelandii has been characterised by X-ray crystallography in both ADP tetrafluoroaluminate-bound [5] and MgATP-bound [6] states. The enzyme possesses molybdenum iron - sulfido cluster cofactors ( FeMoco ) as active sites , each bearing two pseudocubic iron-sulfido structures.
The ribosylation takes place when reduced nitrogen is present and it causes a barrier in the electron transfer flow and thereby inactivates nitrogenase activity. The enzymes catalyzing the ribosylation are called DraG and DraT. [3] [4] Rhodobacter capsulatus—a free-living anaerobic phototroph containing a transcriptional nif gene regulatory ...