期刊
BIOCHEMISTRY
卷 48, 期 31, 页码 7512-7518出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi9002524
关键词
-
资金
- National Institutes of Health [AI072443]
Human NFU (also known as HIRIP5) has been implicated in cellular iron-sulfur cluster biosynthesis. Bacterial and yeast forms arc smaller than the human protein and arc homologous to the C-terminal domain of human NFU. This C-terminal domain contains a pair of redox active cysteines and demonstrates thioiredoxin-like activity by both binding to and mediating persulfide bond cleavage of sulfurloaded IscS, the sulfide donor for [2Fe-2S] cluster assembly oil ISU-type scaffold proteins. Herein, human NFU is shown to possess a novel combination of a molten globule-type C-terminal domain and an N-terminal domain with a fully folded regular tertiary structure. The molten globule characteristics of the C-terminal domain have been evaluated by 1-anilino-8-naphthalenesulfonic acid binding, the kinetics of trypsin digestion, and heteronuclear single-quantum coherence nuclear magnetic resonance Studies. Human NFU is a functionally competent reducing agent for cysteinyl persulfide bond cleavage, releasing inorganic sulfide for incorporation into the ISU-bound [2Fe-2S] cluster, a reactivity that might be facilitated by the flexibility of the C-terminal domain.
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