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Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2
Author(s) -
Beinert Helmut,
Kennedy Mary Claire
Publication year - 1993
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.7.15.8262329
Subject(s) - aconitase , enzyme , electron paramagnetic resonance , chemistry , biochemistry , crystallography , nuclear magnetic resonance , physics
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 the iron regulatory factor or iron‐responsive element binding protein (IRE‐BP). This has led to the realization that IRE‐BP is an alternative form of cytosolic (not of mitochondrial) aconitase that is devoid of its cubane Fe‐S cluster.— Beinert, H., Kennedy, M. C. Aconitase, a two‐faced protein: enzyme and iron regulatory factor. FASEB J. 7: 1442‐1449; 1993.