The [2Fe‐2S] cluster of mitochondrial outer membrane protein mitoNEET has an O2‐regulated nitric oxide access tunnel
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| Titel: | The [2Fe‐2S] cluster of mitochondrial outer membrane protein mitoNEET has an O2‐regulated nitric oxide access tunnel |
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| Autoren: | Thao Nghi Hoang, Meritxell Wu‐Lu, Alberto Collauto, Peter‐Leon Hagedoorn, Madalina Alexandru, Maike Henschel, Shahram Kordasti, Maria Andrea Mroginski, Maxie M. Roessler, Kourosh H. Ebrahimi |
| Quelle: | FEBS Lett Hoang, T N, Wu-Lu, M, Collauto, A, Hagedoorn, P-L, Alexandru, M, Henschel, M, Kordasti, S, Mroginski, M A, Roessler, M M & Ebrahimi, K H 2025, ' The [2Fe-2S] cluster of mitochondrial outer membrane protein mitoNEET has an O 2-regulated nitric oxide access tunnel ', FEBS Letters, vol. 599, no. 7, pp. 952-970 . https://doi.org/10.1002/1873-3468.15097 |
| Verlagsinformationen: | Wiley, 2025. |
| Publikationsjahr: | 2025 |
| Schlagwörter: | Iron-Sulfur Proteins, Iron-Sulfur Proteins/metabolism, Mitochondrial Proteins/metabolism, Pioglitazone, Oxygen/metabolism, Nitric Oxide, Mitochondrial Membranes/metabolism, Mitochondria, Oxygen, Mitochondrial Proteins, Nitric Oxide/metabolism, Mitochondria/metabolism, Mitochondrial Membranes, Humans, Research Article, Signal Transduction |
| Beschreibung: | The mitochondrial outer membrane iron–sulphur ([Fe‐S]) protein mitoNEET has been extensively studied as a target of the anti‐inflammatory and type‐2 diabetes drug pioglitazone and as a protein affecting mitochondrial respiratory rate. Despite these extensive past studies, its molecular function has yet to be discovered. Here, we applied an interdisciplinary approach and discovered an explicit nitric oxide (NO) access site to the mitoNEET [2Fe‐2S] cluster. We found that O2 and pioglitazone block NO access to the cluster, suggesting a molecular function for the mitoNEET [2Fe‐2S] cluster in mitochondrial signal transduction. Our discovery hints at a new pathway via which mitochondria can sense hypoxia through O2 protection of the mitoNEET [2Fe‐2S] cluster, a new paradigm in understanding the importance of [Fe‐S] clusters for gasotransmitter signal transduction in eukaryotes. |
| Publikationsart: | Article Other literature type |
| Dateibeschreibung: | application/pdf |
| Sprache: | English |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.15097 |
| Zugangs-URL: | https://pubmed.ncbi.nlm.nih.gov/39757450 https://kclpure.kcl.ac.uk/portal/en/publications/6322817e-a9de-4c90-9370-22b579294c44 |
| Rights: | CC BY |
| Dokumentencode: | edsair.doi.dedup.....86f98f6ead74c3e2658c5d35bd18e516 |
| Datenbank: | OpenAIRE |
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Nájsť tento článok vo Web of Science | Abstract: | The mitochondrial outer membrane iron–sulphur ([Fe‐S]) protein mitoNEET has been extensively studied as a target of the anti‐inflammatory and type‐2 diabetes drug pioglitazone and as a protein affecting mitochondrial respiratory rate. Despite these extensive past studies, its molecular function has yet to be discovered. Here, we applied an interdisciplinary approach and discovered an explicit nitric oxide (NO) access site to the mitoNEET [2Fe‐2S] cluster. We found that O2 and pioglitazone block NO access to the cluster, suggesting a molecular function for the mitoNEET [2Fe‐2S] cluster in mitochondrial signal transduction. Our discovery hints at a new pathway via which mitochondria can sense hypoxia through O2 protection of the mitoNEET [2Fe‐2S] cluster, a new paradigm in understanding the importance of [Fe‐S] clusters for gasotransmitter signal transduction in eukaryotes. |
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| ISSN: | 18733468 00145793 |
| DOI: | 10.1002/1873-3468.15097 |