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  2. Nitrogenase - Wikipedia

    en.wikipedia.org/wiki/Nitrogenase

    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.

  3. FeMoco - Wikipedia

    en.wikipedia.org/wiki/FeMoco

    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.

  4. Cytochrome - Wikipedia

    en.wikipedia.org/wiki/Cytochrome

    The iron in cytochromes usually exists in a ferrous (Fe 2+) and a ferric (Fe 3+) state with a ferroxo (Fe 4+) state found in catalytic intermediates. [1] Cytochromes are, thus, capable of performing electron transfer reactions and catalysis by reduction or oxidation of their heme iron. The cellular location of cytochromes depends on their function.

  5. Iron–sulfur protein - Wikipedia

    en.wikipedia.org/wiki/Iron–sulfur_protein

    Their formal oxidation states may vary from [Fe 3 S 4] + (all-Fe 3+ form) to [Fe 3 S 4] 2− (all-Fe 2+ form). In a number of iron–sulfur proteins, the [Fe 4 S 4] cluster can be reversibly converted by oxidation and loss of one iron ion to a [Fe 3 S 4] cluster. E.g., the inactive form of aconitase possesses an [Fe 3 S 4] and is activated by ...

  6. Nitrogen fixation - Wikipedia

    en.wikipedia.org/wiki/Nitrogen_fixation

    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]

  7. Molecular orbital theory - Wikipedia

    en.wikipedia.org/wiki/Molecular_orbital_theory

    Molecular orbital diagram of He 2. Bond order is the number of chemical bonds between a pair of atoms. The bond order of a molecule can be calculated by subtracting the number of electrons in anti-bonding orbitals from the number of bonding orbitals, and the resulting number is then divided by two. A molecule is expected to be stable if it has ...

  8. Transition metal dinitrogen complex - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_di...

    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 ...

  9. Nucleotide base - Wikipedia

    en.wikipedia.org/wiki/Nucleotide_base

    Base pairing: Two base pairs are produced by four nucleotide monomers, nucleobases are in blue. Guanine (G) is paired with cytosine (C) via three hydrogen bonds, in red. Adenine (A) is paired with uracil (U) via two hydrogen bonds, in red. Purine nucleobases are fused-ring molecules. Pyrimidine nucleobases are simple ring molecules.