Reactivity, Mechanism, and Assembly of the Alternative Nitrogenases

• Published in: Chemical reviews Vol. 120; no. 12; pp. 5107 - 5157
• Main Authors: Jasniewski, Andrew J, Lee, Chi Chung, Ribbe, Markus W, Hu, Yilin
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 24.06.2020
• Subjects: biosynthesis; catalytic activity; chemical bonding; Chemistry; Cluster chemistry; Crystal structure; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Iron; Models, Molecular; Molybdenum; Molybdenum - chemistry; Molybdenum - metabolism; Monomers; multigene family; Nitrogen; Nitrogen - chemistry; Nitrogen - metabolism; Nitrogen Fixation; nitrogenase; Nitrogenase - chemistry; Nitrogenase - metabolism; Nitrogenation; Peptides and proteins; spectral analysis; Structural analysis

Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated with the molybdenum–iron cofactor called FeMoco or the M-cluster, and it has been the subject of extensive structural...