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

Authors
Yang, KS; Kang, SW; Woo, HA; Hwang, SC; Chae, HZ; Kim, K; Rhee, SG
Citation
The Journal of biological chemistry, 277(41):38029-38036, 2002
Journal Title
The Journal of biological chemistry
ISSN
0021-92581083-351X
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 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).
MeSH terms
Amino Acid SequenceAntioxidants/chemistry/metabolismCatalysis*Catalytic DomainCysteine/*analogs & derivatives/chemistry/*metabolismHela CellsHumansHydrogen Peroxide/metabolismHydrogen-Ion ConcentrationMolecular Sequence DataMutationNADP/*metabolismOxidants/metabolismOxidation-ReductionPeptides/metabolismPeroxidases/chemistry/genetics/*metabolismPeroxiredoxinsRecombinant Proteins/chemistry/genetics/metabolismSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationThioredoxin-Disulfide Reductase/metabolismThioredoxins/metabolism
DOI
10.1074/jbc.M206626200
PMID
12161445
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Medical Science
AJOU Authors
황, 성철
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