Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 강상원 | * |
dc.date.accessioned | 2016-08-28T11:08:40Z | - |
dc.date.available | 2016-08-28T11:08:40Z | - |
dc.date.issued | 2002 | * |
dc.identifier.issn | 0021-9258 | * |
dc.identifier.other | OAK-12621 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/228712 | - |
dc.description.abstract | By following peroxiredoxin I (Prx I)-dependent NADPH oxidation spectrophotometrically, we observed that Prx I activity decreased gradually with time. The decay in activity was coincident with the conversion of Prx I to a more acidic species as assessed by two-dimensional gel electrophoresis. Mass spectral analysis and studies with Cys mutants determined that this shift in pI was due to selective oxidation of the catalytic site Cys51-SH to Cys51-SO2H. Thus, Cys51-SOH generated as an intermediate during catalysis appeared to undergo occasional further oxidation to Cys51-SO2H, which cannot be reversed by thioredoxin. The presence of H2O2 alone was not sufficient to cause oxidation of Cys51 to Cys51-SO2H. Rather, the presence of complete catalytic components (H2O2, thioredoxin, thioredoxin reductase, and NADPH) was necessary, indicating that such hyperoxidation occurs only when Prx I is engaged in the catalytic cycle. Likewise, hyperoxidation of Cys172/Ser172 mutant Prx I required not only H2O2, but also a catalysis-supporting thiol (dithiothreitol). Kinetic analysis of Prx I inactivation in the presence of a low steady-state level (<1 μm) of H2O2 indicated that Prx I was hyperoxidized at a rate of 0.072% per turnover at 30°C. Hyperoxidation of Prx I was also detected in HeLa cells treated with H2O2. | * |
dc.language | English | * |
dc.title | Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid | * |
dc.type | Article | * |
dc.relation.issue | 41 | * |
dc.relation.volume | 277 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 38029 | * |
dc.relation.lastpage | 38036 | * |
dc.relation.journaltitle | Journal of Biological Chemistry | * |
dc.identifier.doi | 10.1074/jbc.M206626200 | * |
dc.identifier.scopusid | 2-s2.0-0037064080 | * |
dc.author.google | Yang K.-S. | * |
dc.author.google | Kang S.W. | * |
dc.author.google | Woo H.A. | * |
dc.author.google | Hwang S.C. | * |
dc.author.google | Chae H.Z. | * |
dc.author.google | Kim K. | * |
dc.author.google | Rhee S.G. | * |
dc.contributor.scopusid | 강상원(55731433900) | * |
dc.date.modifydate | 20240118155300 | * |