Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria
Author:
Affiliation:
1. Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106-4970, and Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira, Aoba-ku, Sendai 980-8577, Japan
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi0353979
Reference61 articles.
1. 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
2. Mitochondrial Aconitase Is a Source of Hydroxyl Radical
3. Rapid inactivation of plant aconitase by hydrogen peroxide
4. Aconitase as Iron−Sulfur Protein, Enzyme, and Iron-Regulatory Protein
5. Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite
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