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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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Main Authors: Pandey, Alok, Gordon, Donna M., Pain, Jayashree, Stemmler, Timothy L., Dancis, Andrew, Pain, Debkumar
格式: Artigo
語言:Inglês
出版: American Society for Biochemistry and Molecular Biology 2013
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在線閱讀: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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