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.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2016 Sept 2|
Bibliographical noteFunding 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 ).
© 2016 Elsevier Inc.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology