ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2012
Competition of zinc ion for the [2Fe-2S] cluster binding site in the diabetes drug target protein mitoNEET.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Targeting the Electron Transport System for Enhanced Longevity.Biomolecules · 2025Review
- Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis inThe Journal of biological chemistry · 2020Article
- Zinc Toxicity and Iron-Sulfur Cluster Biogenesis inApplied and environmental microbiology · 2019Article
- MitoNEET Deficiency Alleviates Experimental Alcoholic Steatohepatitis in Mice by Stimulating Endocrine Adiponectin-Fgf15 Axis.The Journal of biological chemistry · 2016Article
- Accessory NUMM (NDUFS6) subunit harbors a Zn-binding site and is essential for biogenesis of mitochondrial complex I.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase.Free radical biology & medicine · 2015Article
- Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.The Journal of biological chemistry · 2014Article
- CFTR activity and mitochondrial function.Redox biology · 2013Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Human mitochondrial protein mitoNEET is a novel target of type II diabetes drug pioglitazone, and contains a redox active [2Fe-2S] cluster that is hosted by a unique ligand arrangement of three cysteine and one histidine residues. Here we report that zinc ion can compete for the [2Fe-2S] cluster binding site in human mitoNEET and potentially modulate the physiological function of mitoNEET. When recombinant mitoNEET is expressed in Escherichia coli cells grown in M9 minimal media, purified mitoNEET contains very little or no iron-sulfur clusters. Addition of exogenous iron or zinc ion in the media produces mitoNEET bound with a [2Fe-2S] cluster or zinc, respectively. Mutations of the amino acid residues that hosting the [2Fe-2S] cluster in mitoNEET diminish the zinc binding activity, indicating that zinc ion and the [2Fe-2S] cluster may share the same binding site in mitoNEET. Finally, excess zinc ion effectively inhibits the [2Fe-2S] cluster assembly in mitoNEET in E. coli cells, suggesting that zinc ion may impede the function of mitoNEET by blocking the [2Fe-2S] cluster assembly in the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.