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Possible structural analogs for the Fe/M/S sites in the nitrogenases. The[Fe6S6(L)6(M(CO)3)2]n- clusters and the [(MFe3S4)2(μ2-S)(μ2-L)]n- singly- and doubly-bridged double cubanes

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Nitrogen Fixation

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Abstract

The MoFe-protein components in the nitrogenases (31) from various nitrogen-fixing organisms contain a common Fe/Mo/S structural unit that can be isolated as an extractable cofactor (FeMoco) (36). The intimate relation of this cofactor to N2 reduction is provided by the observation mat inactive extracts of derepressed cells of mutant strains, which do not contain FeMoco, are activated upon its addition. The cofactor appears to be a small anionic cluster that does not contain amino acids and may contain homocitrate (26). The determination of its structure has not been as simple a task as it might seem. Indeed, since its isolation nearly 13 years ago, FeMoco still has not been obtained in crystalline form.

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Authors and Affiliations

  1. Dept. of Chemistry, University of Michigan, Ann Arbor, MI, 48106, USA

    D. Coucouvanis

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  1. D. Coucouvanis
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Peter M. Gresshoff L. Evans Roth Gary Stacey William E. Newton

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Coucouvanis, D. (1990). Possible structural analogs for the Fe/M/S sites in the nitrogenases. The[Fe6S6(L)6(M(CO)3)2]n- clusters and the [(MFe3S4)2(μ2-S)(μ2-L)]n- singly- and doubly-bridged double cubanes. In: Gresshoff, P.M., Roth, L.E., Stacey, G., Newton, W.E. (eds) Nitrogen Fixation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6432-0_15

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  • DOI: https://doi.org/10.1007/978-1-4684-6432-0_15

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