Novel Oxidative Modifications in Redox-Active Cysteine Residues

• DOI: 10.1074/mcp.m110.000513
• Publication Date: 2010-12-11T02:36:45Z
• Authors: Jaeho Jeong; Yongsik Jung; Seungjin Na; Jihye Jeong; Eunsun Lee; Mi-Sun Kim; Sun Choi; Dong-Hae Shin; Eunok Paek; Hee-Yoon Lee; Kong-Joo Lee
• Keywords: Oxidation reduction

Redox-active cysteine, a highly reactive sulfhydryl, is one of the major targets ROS. Formation disulfide bonds and other oxidative derivatives cysteine including sulfenic, sulfinic, sulfonic acids, regulates biological function various proteins. We identified novel low-abundant modifications in cellular GAPDH purified on 2-dimensional gel electrophoresis (2D-PAGE) by employing selectively excluded mass screening analysis for nano ultraperformance liquid chromatography-electrospray-quadrupole-time flight tandem spectrometry, conjunction with MODi MODmap algorithm. observed unexpected shifts (Δm=-16, -34, +64, +87, +103 Da) at redox-active residue 2D-PAGE, oxidized NDP kinase A, peroxiredoxin 6, mitochondrial Mass differences -16, +64 Da are presumed to reflect conversion serine, dehydroalanine (DHA), Cys-SO2-SH respectively. To determine plausible pathways formation these products, we prepared model compounds examined hydrolysis hydration thiosulfonate (Cys-S-SO2-Cys) either DHA (Δm=-34 or serine along (Δm=+64 Da). also detected acrylamide adducts sulfenic sulfinic acids (+87 These findings suggest that oxidations take place residues proteins, thiosulfonate, Cys-SO2-SH, DHA, addition cysteine.