Cited 0 times in Scipus Cited Count

Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid.

DC Field Value Language
dc.contributor.authorYang, KS-
dc.contributor.authorKang, SW-
dc.contributor.authorWoo, HA-
dc.contributor.authorHwang, SC-
dc.contributor.authorChae, HZ-
dc.contributor.authorKim, K-
dc.contributor.authorRhee, SG-
dc.date.accessioned2011-07-20T01:20:09Z-
dc.date.available2011-07-20T01:20:09Z-
dc.date.issued2002-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/3469-
dc.description.abstractBy 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 Cys(51)-SH to Cys(51)-SO(2)H. Thus, Cys(51)-SOH generated as an intermediate during catalysis appeared to undergo occasional further oxidation to Cys(51)-SO(2)H, which cannot be reversed by thioredoxin. The presence of H(2)O(2) alone was not sufficient to cause oxidation of Cys(51) to Cys(51)-SO(2)H. Rather, the presence of complete catalytic components (H(2)O(2), 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 Cys(172)/Ser(172) mutant Prx I required not only H(2)O(2), but also a catalysis-supporting thiol (dithiothreitol). Kinetic analysis of Prx I inactivation in the presence of a low steady-state level (<1 microm) of H(2)O(2) indicated that Prx I was hyperoxidized at a rate of 0.072% per turnover at 30 degrees C. Hyperoxidation of Prx I was also detected in HeLa cells treated with H(2)O(2).-
dc.language.isoen-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHAntioxidants-
dc.subject.MESHCatalysis-
dc.subject.MESHCatalytic Domain-
dc.subject.MESHCysteine-
dc.subject.MESHHela Cells-
dc.subject.MESHHumans-
dc.subject.MESHHydrogen Peroxide-
dc.subject.MESHHydrogen-Ion Concentration-
dc.subject.MESHMolecular Sequence Data-
dc.subject.MESHMutation-
dc.subject.MESHNADP-
dc.subject.MESHOxidants-
dc.subject.MESHOxidation-Reduction-
dc.subject.MESHPeptides-
dc.subject.MESHPeroxidases-
dc.subject.MESHPeroxiredoxins-
dc.subject.MESHRecombinant Proteins-
dc.subject.MESHSpectrometry, Mass, Electrospray Ionization-
dc.subject.MESHSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization-
dc.subject.MESHThioredoxin-Disulfide Reductase-
dc.subject.MESHThioredoxins-
dc.titleInactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid.-
dc.typeArticle-
dc.identifier.pmid12161445-
dc.identifier.urlhttp://www.jbc.org/cgi/pmidlookup?view=long&pmid=12161445-
dc.contributor.affiliatedAuthor황, 성철-
dc.type.localJournal Papers-
dc.identifier.doi10.1074/jbc.M206626200-
dc.citation.titleThe Journal of biological chemistry-
dc.citation.volume277-
dc.citation.number41-
dc.citation.date2002-
dc.citation.startPage38029-
dc.citation.endPage38036-
dc.identifier.bibliographicCitationThe Journal of biological chemistry, 277(41). : 38029-38036, 2002-
dc.identifier.eissn1083-351X-
dc.relation.journalidJ000219258-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Medical Science
Files in This Item:
There are no files associated with this item.

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse