Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2

@article{Beinert1993AconitaseAT,
  title={Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2},
  author={Helmut Beinert and Mary Claire Kennedy},
  journal={The FASEB Journal},
  year={1993},
  volume={7},
  pages={1442 - 1449}
}
In this brief survey, the path of development of our knowledge of the iron‐sulfur enzyme aconitase [citrate(isocitrate)hydrolyase EC4.2.1.3.] is traced from its discovery in 1937, Particular emphasis is on developments in the past decade, when EPR, Mössbauer and electron nuclear double resonance spectroscopies, X‐ray crystallography, and mutational analysis were applied to the problem. More recently discovered was the significant amino acid sequence identity between mitochondrial aconitase and… 
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The capacity of physiological reducing systems to cooperate with NO in the activation of IRP1 and the combined effect of NO and Trx on IRP2, which exhibits constitutive RNA binding activity are examined.
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Mechanisms of Fe–S biogenesis and delivery, and methods that will likely reveal important roles of Fe—S proteins in proteins not yet recognized as Fe-S proteins are discussed.
Iron regulatory proteins 1 and 2
  • B. Henderson
  • Biology, Medicine
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1996
TLDR
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Modulation of Iron Regulatory Protein Functions
TLDR
Results imply that neither O nor ONOO can convert [4Fe-4S] IRP into IRE-binding protein but rather suggest that an active redox form of NO converts IRp into its IRE binding form by targeting the [Fe-S] cluster.
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TLDR
The amino acid composition, molecular weight, isoelectric point, and the sequences of six random peptides clearly show that these physicochemical and structural characteristics are identical to those of IRE-BP, and that c-aconitase is distinctly different from m-aconitic aconitase.
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TLDR
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TLDR
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