The Outer Mitochondrial Membrane Protein Mitoneet Contains a Novel Redox-active 2fe-2s Cluster.
From: Department of Pharmacology, University of California, San Diego, La Jolla, California 92093, USA.
The Journal of biological chemistry
- Publish Date: Aug 2007
- ISSN: 0021-9258
- Volume: 282
- Issue: 33
- Pages: 23745-9
- Medium: Print
- Language: English
- Citation (JAMA): Wiley Sandra E, Paddock Mark L, Abresch Edward C, et al. The Outer Mitochondrial Membrane Protein Mitoneet Contains a Novel Redox-active 2fe-2s Cluster.. J. Biol. Chem. Aug 2007;282:23745-9
Abstract
The outer mitochondrial membrane protein mitoNEET was discovered as a binding target of pioglitazone, an insulin-sensitizing drug of the thiazolidinedione class used to treat type 2 diabetes (Colca, J. R., McDonald, W. G., Waldon, D. J., Leone, J. W., Lull, J. M., Bannow, C. A., Lund, E. T., and Mathews, W. R.(2004) Am. J. Physiol. 286, E252-E260). We have shown that mitoNEET is a member of a small family of proteins containing a 39-amino-acid CDGSH domain. Although the CDGSH domain is annotated as a zinc finger motif, mitoNEET was shown to contain iron (Wiley, S. E., Murphy, A. N., Ross, S. A., van der Geer, P., and Dixon, J. E.(2007) Proc. Natl. Acad. Sci. U. S. A. 104, 5318-5323). Optical and electron paramagnetic resonance spectroscopy showed that it contained a redox-active pH-labile Fe-S cluster. Mass spectrometry showed the loss of 2Fe and 2S upon cofactor extrusion. Spectroscopic studies of recombinant proteins showed that the 2Fe-2S cluster was coordinated by Cys-3 and His-1. The His ligand was shown to be involved in the observed pH lability of the cluster, indicating that loss of this ligand via protonation triggered release of the cluster. mitoNEET is the first identified 2Fe-2S-containing protein located in the outer mitochondrial membrane. Based on the biophysical data and domain fusion analysis, mitoNEET may function in Fe-S cluster shuttling and/or in redox reactions.
Mesh Headings (Keywords): Binding Sites, Cysteine, Histidine, Humans, Hydrogen-Ion Concentration, Iron-Binding Proteins, Iron-Sulfur Proteins, Membrane Proteins, Mitochondrial Membranes, Mitochondrial Proteins, Oxidation-Reduction, Spectrum Analysis, Zinc Fingers
Check for Full Text / PubMed Unique Identifier (PMID): 17584744
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.