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FeMoco information


Structure of the FeMo cofactor showing the sites of binding to nitrogenase[1] The amino acids cysteine (Cys) and histidine (His) are indicated.

FeMoco (FeMo cofactor) is the primary cofactor of nitrogenase. Nitrogenase is the enzyme that catalyzes the conversion of atmospheric nitrogen molecules N2 into ammonia (NH3) through the process known as nitrogen fixation. Studying FeMoco's role in the reaction mechanism for nitrogen fixation is a potential use case for quantum computers. Even limited quantum computers could enable better simulations of the reaction mechanism.[2] Because it contains iron and molybdenum, the cofactor is called FeMoco. Its stoichiometry is Fe7MoS9C.

  1. ^ Einsle O, Rees DC (June 2020). "Structural Enzymology of Nitrogenase Enzymes". Chemical Reviews. 120 (12): 4969–5004. doi:10.1021/acs.chemrev.0c00067. PMC 8606229. PMID 32538623. S2CID 219703833.
  2. ^ Reiher M, Wiebe N, Svore KM, Wecker D, Troyer M (July 2017). "Elucidating reaction mechanisms on quantum computers". Proceedings of the National Academy of Sciences of the United States of America. 114 (29): 7555–7560. arXiv:1605.03590. Bibcode:2017PNAS..114.7555R. doi:10.1073/pnas.1619152114. PMC 5530650. PMID 28674011.

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