ArticleBiochemistry2011
Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Inhibition of Glucose-Induced Glycation of HSA by Pioglitazone: Multi-Spectroscopic and Bioinformatic Evidence.Molecules (Basel, Switzerland) · 2026Article
- Medicinal Chemistry Review of the NEET Protein Family.ChemMedChem · 2026Review
- Iron-sulfur cluster redox chemistry and dimer dissociation in the outer mitochondrial membrane protein, mitoNEET.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Development of a fluorescence screening assay for binding partners of the iron-sulfur mitochondrial protein mitoNEET.Bioorganic & medicinal chemistry letters · 2023Article
- Multiple Poses and Thermodynamics of Ligands Targeting Protein Surfaces: The Case of Furosemide Binding to mitoNEET in Aqueous Solution.Frontiers in cell and developmental biology · 2022Article
- The two redox states of the human NEET proteins' [2Fe-2S] clusters.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Development of Drug Dual-Carriers Delivery System with Mitochondria-Targeted and pH/Heat Responsive Capacity for Synergistic Photothermal-Chemotherapy of Ovarian Cancer.International journal of nanomedicine · 2020Article
- Binding of thiazolidinediones to the endoplasmic reticulum protein nutrient-deprivation autophagy factor-1.Bioorganic & medicinal chemistry letters · 2019Article
- Crystal structure of the mitochondrial protein mitoNEET bound to a benze-sulfonide ligand.Communications chemistry · 2019Article
- Molecular Dynamics Simulations of the [2Fe-2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release.The journal of physical chemistry. B · 2017Article
- Identification of small molecules that bind to the mitochondrial protein mitoNEET.Bioorganic & medicinal chemistry letters · 2016Article
- Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.The Journal of biological chemistry · 2014Article
- Competition of zinc ion for the [2Fe-2S] cluster binding site in the diabetes drug target protein mitoNEET.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Binding of the thiazolidinedione antidiabetic drug pioglitazone led to the discovery of a novel outer mitochondrial membrane protein of unknown function called mitoNEET. The protein is homodimeric and contains a uniquely ligated two iron-two sulfur cluster in each of its two cytosolic domains. Electrospray ionization mass spectrometry was employed to characterize solutions of the soluble cytosolic domain (amino acids 32--108) of the protein. Ions characteristic of dimers containing the cofactors were readily detected under native conditions. mitoNEET responded to exposure to solutions at low pH by dissociation to give monomers that retained the cofactor, followed by dissociation of the cofactor in a concerted fashion. mitoNEET formed complexes with resveratrol-3-sulfate, one of the primary metabolites of the natural product resveratrol. Resveratrol itself showed no tendency to interact with mitoNEET. The formation of complexes was evident in both electrospray ionization mass spectrometry and isothermal titration calorimetry measurements. Up to eight molecules of the compound associated with the dimeric form of the protein in a sequential fashion. Dissociation constants determined by micorcalorimetry were in the range 5-16 μM for the various binding sites. The only other known naturally occurring binding partner for mitoNEET at present is NADPH. It is very interesting that the iron-sulfur cluster containing protein interacts with two potentially redox active substances at the surface of mitochondria. These findings provide a new direction for research into two poorly understood, yet biomedically relevant, species.
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