作者
Alok Pandey, Donna M Gordon, Jayashree Pain, Timothy L Stemmler, Andrew Dancis, Debkumar Pain
发表日期
2013/12/27
期刊
Journal of Biological Chemistry
卷号
288
期号
52
页码范围
36773-36786
出版商
American Society for Biochemistry and Molecular Biology
简介
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 manner depending on the accessory protein Isd11. The persulfide is then transferred to the scaffold Isu, where it combines with iron to form the Fe-S cluster intermediate. Frataxin is implicated in the process, although it is unclear where and how, and deficiency causes Friedreich ataxia. Using purified proteins and isolated mitochondria, we show here that the yeast frataxin homolog (Yfh1) directly and specifically stimulates cysteine binding to Nfs1 by exposing substrate-binding sites. This novel function of frataxin does not require iron, Isu1, or Isd11. Once bound to Nfs1, the substrate cysteine is the source of the Nfs1 persulfide …
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A Pandey, DM Gordon, J Pain, TL Stemmler, A Dancis… - Journal of Biological Chemistry, 2013