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Frataxin Directly Stimulates Mitochondrial Cysteine Desulfurase by Exposing Substrate-binding Sites, and a Mutant Fe-S Cluster Scaffold Protein with Frataxin-bypassing Ability Acts Similarly
For iron-sulfur (Fe-S) cluster synthesis in mitochondria, the sulfur is derived from the amino acid cysteine by the cysteine desulfurase activity of Nfs1. The enzyme binds the substrate cysteine in the pyridoxal phosphate-containing site, and a persulfide is formed on the active site cysteine in a m...
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| Autores principales: | , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2013
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3873537/ https://ncbi.nlm.nih.gov/pubmed/24217246 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.525857 |
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