Crystal structures of human peroxiredoxin 6 in different oxidation states

Kyung Hee Kim; Weontae Lee; Eunice Eun Kyeong Kim

doi:10.1016/j.bbrc.2016.06.125

Crystal structures of human peroxiredoxin 6 in different oxidation states

Kyung Hee Kim, Weontae Lee, Eunice Eun Kyeong Kim

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

Peroxiredoxins (Prxs) are a family of antioxidant enzymes found ubiquitously. Prxs function not only as H₂O₂ scavengers but also as highly sensitive H₂O₂ sensors and signal transducers. Since reactive oxygen species are involved in many cellular metabolic and signaling processes, Prxs play important roles in various diseases. Prxs can be hyperoxidized to the sulfinic acid ([Formula presented]₂H) or sulfonic acid ([Formula presented]₃H) forms in the presence of high concentrations of H₂O₂. It is known that oligomerization of Prx is changed accompanying oxidation states, and linked to the function. Among the six Prxs in mammals, Prx6 is the only 1-Cys Prx. It is found in all organs in humans, unlike some 2-Cys Prxs, and is present in all species from bacteria to humans. In addition, Prx6 has Ca²⁺-independent phospholipase A₂ (PLA₂) activity. Thus far only the crystal structure of Prx in the oxidized state has been reported. In this study, we present the crystal structures of human Prx6 in the reduced (SH) and the sulfinic acid (SO₂H) forms.

Original language	English
Pages (from-to)	717-722
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	477
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2016.06.125
Publication status	Published - 2016 Sept 2

Bibliographical note

Funding Information:
We thank staff at 4A beamline, Pohang Accelerator Laboratory, Korea. This work was supported by grant from the Global Research Laboratory (GRL) program of the Ministry of Science, ICT and Future Planning of Korea (MISP: grant No. NRF 20110021713 ), and grant from Korea Institute of Science and Technology ( 2E26360 ).

Publisher Copyright:
© 2016 Elsevier Inc.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bbrc.2016.06.125

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title = "Crystal structures of human peroxiredoxin 6 in different oxidation states",

abstract = "Peroxiredoxins (Prxs) are a family of antioxidant enzymes found ubiquitously. Prxs function not only as H2O2 scavengers but also as highly sensitive H2O2 sensors and signal transducers. Since reactive oxygen species are involved in many cellular metabolic and signaling processes, Prxs play important roles in various diseases. Prxs can be hyperoxidized to the sulfinic acid ([Formula presented]2H) or sulfonic acid ([Formula presented]3H) forms in the presence of high concentrations of H2O2. It is known that oligomerization of Prx is changed accompanying oxidation states, and linked to the function. Among the six Prxs in mammals, Prx6 is the only 1-Cys Prx. It is found in all organs in humans, unlike some 2-Cys Prxs, and is present in all species from bacteria to humans. In addition, Prx6 has Ca2+-independent phospholipase A2 (PLA2) activity. Thus far only the crystal structure of Prx in the oxidized state has been reported. In this study, we present the crystal structures of human Prx6 in the reduced (SH) and the sulfinic acid (SO2H) forms.",

author = "Kim, {Kyung Hee} and Weontae Lee and Kim, {Eunice Eun Kyeong}",

note = "Funding Information: We thank staff at 4A beamline, Pohang Accelerator Laboratory, Korea. This work was supported by grant from the Global Research Laboratory (GRL) program of the Ministry of Science, ICT and Future Planning of Korea (MISP: grant No. NRF 20110021713 ), and grant from Korea Institute of Science and Technology ( 2E26360 ). Publisher Copyright: {\textcopyright} 2016 Elsevier Inc.",

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AU - Kim, Eunice Eun Kyeong

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N2 - Peroxiredoxins (Prxs) are a family of antioxidant enzymes found ubiquitously. Prxs function not only as H2O2 scavengers but also as highly sensitive H2O2 sensors and signal transducers. Since reactive oxygen species are involved in many cellular metabolic and signaling processes, Prxs play important roles in various diseases. Prxs can be hyperoxidized to the sulfinic acid ([Formula presented]2H) or sulfonic acid ([Formula presented]3H) forms in the presence of high concentrations of H2O2. It is known that oligomerization of Prx is changed accompanying oxidation states, and linked to the function. Among the six Prxs in mammals, Prx6 is the only 1-Cys Prx. It is found in all organs in humans, unlike some 2-Cys Prxs, and is present in all species from bacteria to humans. In addition, Prx6 has Ca2+-independent phospholipase A2 (PLA2) activity. Thus far only the crystal structure of Prx in the oxidized state has been reported. In this study, we present the crystal structures of human Prx6 in the reduced (SH) and the sulfinic acid (SO2H) forms.

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Crystal structures of human peroxiredoxin 6 in different oxidation states

Abstract

Bibliographical note

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UN SDGs

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