Human Cytoplasmic Aconitase (Iron Regulatory Protein 1) Is Converted into Its [3Fe-4S] Form by Hydrogen Peroxide in Vitro but Is Not Activated for Iron-responsive Element Binding
Open Access
- 1 July 1999
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (31) , 21625-21630
- https://doi.org/10.1074/jbc.274.31.21625
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- Mitochondrial EvolutionScience, 1999
- Inactivation of Both RNA Binding and Aconitase Activities of Iron Regulatory Protein-1 by Quinone-induced Oxidative StressJournal of Biological Chemistry, 1999
- Regulation of Mammalian Iron Metabolism: Current State and Need for Further KnowledgeCritical Reviews in Clinical Laboratory Sciences, 1997
- Iron-sulfur clusters and oxidant stress responsesTrends in Biochemical Sciences, 1996
- Iron-sulfur clusters as biosensors of oxidants and ironTrends in Biochemical Sciences, 1996
- Expression and Βiochemical Characterization of Iron Regulatory Proteins 1 and 2 in Saccharomyces cerevisiaeBiochemistry, 1996
- Human ferrochelatase is an iron-sulfur proteinBiochemistry, 1994
- On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe–4S] ferredoxinProtein Engineering, Design and Selection, 1994
- Biologically relevant metal ion‐dependent hydroxyl radical generation An updateFEBS Letters, 1992
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976