Plausible structure of the iron-molybdenum cofactor of nitrogenase

Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6487-91. doi: 10.1073/pnas.89.14.6487.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Formates / chemistry
  • In Vitro Techniques
  • Molecular Structure
  • Molybdoferredoxin / ultrastructure*
  • Nitrogenase / metabolism
  • Nitrogenase / ultrastructure*
  • Oxidation-Reduction
  • Structure-Activity Relationship
  • Substrate Specificity
  • Tricarboxylic Acids / chemistry

Substances

  • Formates
  • Molybdoferredoxin
  • Tricarboxylic Acids
  • homocitric acid
  • Nitrogenase