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- W2152320879 abstract "The role of Fe protein in nitrogenase catalysis seems to be understood (Mortenson, Thorneley, 1979; Hageman, Burris, 1980). Fe protein contains a [4Fe-4S] cluster that functions as a one electron donor. Reduced Fe protein, MoFe protein and two MgATP rapidly form a ternary complex. In the complex, ATP hydrolysis is coupled to electron transfer from Fe protein to MoFe protein (Eady et al., 1978) and it has been calculated that two MgATP molecules are hydrolyzed for each electron transferred (Hageman et al., 1980). The rate of electron transfer is relatively fast compared to the flux of electrons through nitrogenase during turnover (Thorneley, 1975). After electron transfer, the slowest step in the cycle of nitrogenase catalysis occurs: that of dissociation of oxidized Fe protein from MoFe protein (Thorneley, Lowe, 1983). Dissociation is necessary because it has been suggested that Fe protein cannot be reduced when bound to MoFe protein (Hageman, Burris, 1978)." @default.
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- W2152320879 date "1985-01-01" @default.
- W2152320879 modified "2023-09-24" @default.
- W2152320879 title "The Role of Fe Protein in Nitrogenase Catalysis" @default.
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- W2152320879 doi "https://doi.org/10.1007/978-94-009-5175-4_78" @default.
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