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Iron−Sulfur Cluster Biosynthesis: Characterization of a Molten Globule Domain in Human NFU
2009
Biochemistry
Human NFU (also known as HIRIP5) has been implicated in cellular iron-sulfur cluster biosynthesis. Bacterial and yeast forms are smaller than the human protein and are homologous to the C-terminal domain of human NFU. This C-terminal domain contains a pair of redox active cysteines and demonstrates thioredoxin-like activity by both binding to and mediating persulfide bond cleavage of sulfur-loaded IscS; the sulfide donor for [2Fe-2S] cluster assembly on ISU-type scaffold proteins. Herein, human
doi:10.1021/bi9002524
pmid:19722697
pmcid:PMC2766508
fatcat:gcanxm7dp5eplcp2atnzuuauzy