光诱导的 Miner2 线粒体蛋白中与一氧化氮结合的 CDGSH 型[2Fe-2S]簇释放一氧化氮。
Light-induced release of nitric oxide from the nitric oxide-bound CDGSH-type [2Fe-2S] clusters in mitochondrial protein Miner2.
机构信息
Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, 70803, USA.
Department of Chemistry, Louisiana State University, Baton Rouge, LA, 70803, USA.
出版信息
Nitric Oxide. 2019 Aug 1;89:96-103. doi: 10.1016/j.niox.2019.05.007. Epub 2019 May 28.
Human mitochondrial matrix protein Miner2 hosts two [2Fe-2S] clusters via two CDGSH (Cys-Asp-Gly-Ser-His) motifs. Unlike other iron-sulfur clusters in proteins, the reduced CDGSH-type [2Fe-2S] clusters in Miner2 are able to bind nitric oxide (NO) and form stable NO-bound [2Fe-2S] clusters without disruption of the clusters. Here we report that the NO-bound Miner2 [2Fe-2S] clusters can quickly release NO upon the visible light excitation. The UV-visible and Electron Paramagnetic Resonance (EPR) measurements show that the NO-bound Miner2 [2Fe-2S] clusters are converted to the reduced Miner2 [2Fe-2S] clusters upon the light excitation under anaerobic conditions, suggesting that NO binding in the reduced Miner2 [2Fe-2S] clusters is reversible. Additional studies reveal that binding of NO effectively inhibits the redox transition of the Miner2 [2Fe-2S] clusters, indicating that NO may modulate the physiological activity of Miner2 in mitochondria by directly binding to the CDGSH-type [2Fe-2S] clusters in the protein.
人类线粒体基质蛋白 Miner2 通过两个 CDGSH（半胱氨酸-天冬氨酸-甘氨酸-丝氨酸-组氨酸）基序来承载两个 [2Fe-2S] 簇。与蛋白质中的其他铁硫簇不同，Miner2 中的还原型 CDGSH 型 [2Fe-2S] 簇能够结合一氧化氮（NO）并形成稳定的 NO 结合 [2Fe-2S] 簇，而不会破坏簇。在这里，我们报告说，NO 结合的 Miner2 [2Fe-2S] 簇在可见光激发下可以快速释放 NO。紫外可见和电子顺磁共振（EPR）测量表明，在厌氧条件下，光激发下 NO 结合的 Miner2 [2Fe-2S] 簇转化为还原型 Miner2 [2Fe-2S] 簇，表明还原型 Miner2 [2Fe-2S] 簇中的 NO 结合是可逆的。进一步的研究表明，NO 的结合有效地抑制了 Miner2 [2Fe-2S] 簇的氧化还原跃迁，表明 NO 可能通过直接结合蛋白质中的 CDGSH 型 [2Fe-2S] 簇来调节 Miner2 在线粒体中的生理活性。
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