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. 1992 Jul 15;89(14):6487–6491. doi: 10.1073/pnas.89.14.6487

Plausible structure of the iron-molybdenum cofactor of nitrogenase.

M S Madden 1, A M Krezel 1, R M Allen 1, P W Ludden 1, V K Shah 1
PMCID: PMC49526  PMID: 1631147

Abstract

A plausible structure of the iron-molybdenum cofactor of nitrogenase [reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolyzing), EC 1.18.6.1] is presented based on altered substrate reduction properties of dinitrogenase containing homocitrate analogs within the cofactor. Alterations on each carbon of the four-carbon homocitrate backbone were correlated with altered substrate reduction properties of dinitrogenase containing these analogs. Altered substrate reduction properties are the basis for a model in which homocitrate is oriented about two cubane metal clusters.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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