Plausible structure of the iron-molybdenum cofactor of nitrogenase

M. S. Madden, A. M. Krezel, R. M. Allen, P. W. Ludden, V. K. Shah

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish
Pages (from-to)6487-6491
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number14
DOIs
StatePublished - 1992

Keywords

  • bicubane
  • homocitrate

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