Add time:07/13/2019         Source:sciencedirect.com

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.

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