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CAS: 459426-22-3
MF: C25H40N4O10S
MW: 588.6709
Synonyms:  

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Matthew B. Francis

University of California
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Erin K. O'Shea

Harvard University
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Bradley Lether Pentelute

Massachusetts Institute of Technology
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David A. Tirrell

California Institute of Technology
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Christine A. Hrycyna

Purdue University
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David W. Wright

Vanderbilt University
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Dehua Pei

The Ohio State University
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Carlito B. Lebrilla

University of California
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Peter T.A. Reilly

Washington State University
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Kate S. Carroll

The Scripps Research Institute
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Co-reporter: Mauro Lo Conte, Jiusheng Lin, Mark A. Wilson, and Kate S. Carroll
pp: 1825
Publication Date(Web):June 3, 2015
DOI: 10.1021/acschembio.5b00124
Protein sulfinic acids are formed by the reaction of reactive oxygen species with protein thiols. Sulfinic acid formation has long been considered an irreversible state of oxidation and is associated with high cellular oxidative stress. Increasing evidence, however, indicates that cysteine is oxidized to sulfinic acid in cells to a greater extent, and is more controlled, than first thought. The discovery of sulfiredoxin has demonstrated that cysteine sulfinic acid can be reversed, pointing to a vast array of potential implications for redox biology. Identification of the site of protein sulfinylation is crucial in clarifying the physiological and pathological effects of post-translational modifications. Currently, the only methods for detection of sulfinic acids involve mass spectroscopy and the use of specific antibodies. However, these methodologies are not suitable for proteomic studies. Herein, we report the first probe for detection of protein sulfinylation, NO-Bio, which combines a C-nitroso warhead for rapid labeling of sulfinic acid with a biotin handle. Based on this new tool, we developed a selective two-step approach. In the first, a sulfhydryl-reactive compound is introduced to selectively block free cysteine residues. Thereafter, the sample is treated with NO-Bio to label sulfinic acids. This new technology represents a rapid, selective, and general technology for sulfinic acid detection in biological samples. As proof of our concept, we also evaluated protein sulfinylation levels in various human lung tumor tissue lysates. Our preliminary results suggest that cancer tissues generally have higher levels of sulfinylation in comparison to matched normal tissues. A new ability to monitor protein sulfinylation directly should greatly expand the impact of sulfinic acid as a post-translational modification.