Mitochondria are cellular sites of diverse redox biology, including ROS production, iron-sulfur biogenesis, and secondary metabolism, which all rely on proteogenic reactive cysteine residues. Mass spectrometry-based proteomic methods to monitor the reactivity and functionality of cysteine residues across complex proteomes have greatly expanded over the past decade. Here we describe a mitochondrial isolation procedure coupled with cysteine-reactive IA labeling that affords identification and characterization of functional mitochondrial cysteine residues that were heretofore inaccessible to whole-cell proteomic analysis.
CITATION STYLE
Bak, D. W., & Weerapana, E. (2019). Interrogation of functional mitochondrial cysteine residues by quantitative mass spectrometry. In Methods in Molecular Biology (Vol. 1967, pp. 211–227). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9187-7_13
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