期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 21, 期 7, 页码 825-836出版社
SPRINGER
DOI: 10.1007/s00775-016-1381-8
关键词
Mitochondrial disease; Metalloprotein; Iron-sulfur cluster; Cluster exchange; Nfu
资金
- National Institutes of Health [AI072443]
- NIH Chemistry/Biology Interface training grant [T32 GM095450]
Human Nfu is an iron-sulfur cluster protein that has recently been implicated in multiple mitochondrial dysfunctional syndrome (MMDS1). The Nfu family of proteins shares a highly homologous domain that contains a conserved active site consisting of a CXXC motif. There is less functional conservation between bacterial and human Nfu proteins, particularly concerning their Iron-sulfur cluster binding and transfer roles. Herein, we characterize the cluster exchange chemistry of human Nfu and its capacity to bind and transfer a [2Fe-2S] cluster. The mechanism of cluster uptake from a physiologically relevant [2Fe-2S](GS)(4) cluster complex, and extraction of the Nfu-bound iron-sulfur cluster by glutathione are described. Human holo Nfu shows a dimer-tetramer equilibrium with a protein to cluster ratio of 2:1, reflecting the Nfu-bridging [2Fe-2S] cluster. This cluster can be transferred to apo human ferredoxins at relatively fast rates, demonstrating a direct role for human Nfu in the process of [2Fe-2S] cluster trafficking and delivery.
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