Title : Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin.

Pub. Date : 2019 Aug 8

PMID : 31395877






5 Functional Relationships(s)
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Protein Name
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1 Fe-S clusters are biosynthesized on the scaffold protein ISCU, with cysteine desulfurase NFS1 providing sulfur as persulfide and ferredoxin FDX2 supplying electrons, in a process stimulated by FXN but not clearly understood. Iron iron-sulfur cluster assembly enzyme Homo sapiens
2 Here, we report the breakdown of this process, made possible by removing a zinc ion in ISCU that hinders iron insertion and promotes non-physiological Fe-S cluster synthesis from free sulfide in vitro. Iron iron-sulfur cluster assembly enzyme Homo sapiens
3 Here, we report the breakdown of this process, made possible by removing a zinc ion in ISCU that hinders iron insertion and promotes non-physiological Fe-S cluster synthesis from free sulfide in vitro. Iron iron-sulfur cluster assembly enzyme Homo sapiens
4 By binding zinc-free ISCU, iron drives persulfide uptake from NFS1 and allows persulfide reduction into sulfide by FDX2, thereby coordinating sulfide production with its availability to generate Fe-S clusters. Iron iron-sulfur cluster assembly enzyme Homo sapiens
5 By binding zinc-free ISCU, iron drives persulfide uptake from NFS1 and allows persulfide reduction into sulfide by FDX2, thereby coordinating sulfide production with its availability to generate Fe-S clusters. Iron iron-sulfur cluster assembly enzyme Homo sapiens