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  2. 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.

  3. 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.

  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. Serena DeBeer - Wikipedia

    en.wikipedia.org/wiki/Serena_DeBeer

    A strong focus of her research is to study the enzyme that is responsible for the conversion of dinitrogen (N 2) to ammonia (NH 3)—Nitrogenase. Serena DeBeer and her group study this remarkable system comprising a FeMo cofactor (FeMoco) as its active site, and structural model complexes utilizing high-resolution X-ray absorption (XAS) and X ...

  6. Douglas C. Rees - Wikipedia

    en.wikipedia.org/wiki/Douglas_C._Rees

    [3] [4] He examines the structure and function of metal-containing proteins, especially nitrogenase in biological nitrogen fixation, and membrane proteins that carry out ATP-dependent transport through membranes (e.g. ABC transporters). To do this, his group uses X-ray crystallography. His interest in nitrogenase began in William Lipscomb's ...

  7. Azotobacter vinelandii - Wikipedia

    en.wikipedia.org/wiki/Azotobacter_vinelandii

    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.

  8. CPK coloring - Wikipedia

    en.wikipedia.org/wiki/CPK_coloring

    [3] Column K is that of Koltun's patent. [4] Column J is the color scheme used by the molecular visualizer Jmol. [9] Column R is the scheme used by Rasmol; when two colors are shown, the second one is valid for versions 2.7.3 and later. [9] [10] Column P consists of the colors in the PubChem database managed by the United States National ...

  9. Mechanically interlocked molecular architectures - Wikipedia

    en.wikipedia.org/wiki/Mechanically_interlocked...

    On the molecular level, the interlocked molecules cannot be separated without the breaking of the covalent bonds that comprise the conjoined molecules; this is referred to as a mechanical bond. Examples of mechanically interlocked molecular architectures include catenanes , rotaxanes , molecular knots , and molecular Borromean rings .