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Dual role of the active-center cysteine in human peroxiredoxin 1 : Peroxidase activity and heme binding

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Title: Dual role of the active-center cysteine in human peroxiredoxin 1 : Peroxidase activity and heme binding
Authors: Watanabe, Yuta Browse this author
Ishimori, Koichiro Browse this author
Uchida, Takeshi Browse this author →KAKEN DB
Keywords: Heme
Cytosolic heme-binding protein
Issue Date: 12-Feb-2017
Publisher: Elsevier
Journal Title: Biochemical and biophysical research communications
Volume: 483
Issue: 3
Start Page: 930
End Page: 935
Publisher DOI: 10.1016/j.bbrc.2017.01.034
PMID: 28082197
Abstract: HBP23, a 23-kDa heme-binding protein identified in rats, is a member of the peroxiredoxin (Prx) family, the primary peroxidases involved in hydrogen peroxide catabolism. Although HBP23 has a characteristic Cys-Pro heme-binding motif, the significance of heme binding to Prx family proteins remains to be elucidated. Here, we examined the effect of heme binding to human peroxiredoxin-1 (PRX1), which has 97% amino acid identity to HBP23. PRX1 was expressed in Escherichia coli and purified to homogeneity. Spectroscopic titration demonstrated that PRX1 binds heme with a 1:1 stoichiometry and a dissociation constant of 0.17 mu M. UV-vis spectra of heme-PRX1 suggested that Cys52 is the axial ligand of ferric heme. PRX1 peroxidase activity was lost upon heme binding, reflecting the fact that Cys52 is not only the heme-binding site but also the active center of peroxidase activity. Interestingly, heme binding to PRX1 caused a decrease in the toxicity and degradation of heme, significantly suppressing H2O2-dependent heme peroxidase activity and degradation of PRX1-bound heme compared with that of free hemin. By virtue of its cytosolic abundance (similar to 20 mu M), PRX1 thus functions as a scavenger of cytosolic hemin (<1 mu M). Collectively, our results indicate that PRX1 has a dual role; Cys-dependent peroxidase activity and cytosolic heme scavenger. (C) 2017 Elsevier Inc. All rights reserved.
Rights: © 2017. This manuscript version is made available under the CC-BY-NC-ND 4.0 license
Type: article (author version)
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 内田 毅

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