• Geophysics and Geophysical Exploration
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• v.12 no.3
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• pp.225-232
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• 2009

As part of seismic experiments investigating crustal velocity structures of the Korean peninsula, permanent (fixed) seismographs of the Korea Meteorological Administration (KMA) network recorded seismic signals from four and eight large explosions in Korean Crustal Research Team (KCRT) profiles shot in 2004 and 2008, respectively. Among the seismograms recorded by 43 velocity sensors and 103 accelerometers at KMA stations distributed throughout the southern Korean Peninsula, 156 records with epicentral distances less than 120 km and high signal-to-noise ratios were analyzed to determine velocity anisotropy of the Pg phase. Relative elevation corrections of -101.6 to 105.3 ms were made using velocity information derived from the 2004 KCRT profile data and differences in elevation between the permanent KMA stations and the temporary stations in the KCRT profiles at the same source-receiver offsets. To remove site effects, receiver-station corrections of -89.6 to 192.2 ms were additionally made to the KMA station data by subtracting the average differences in traveltimes between KMA stations and portable stations at the same offsets for all available shots with different azimuths. With the exception of anomalously fast velocities along trends of the Chugaryeong fault zone and the Okchon fold belt and anomalously slow velocities in the regions of high terrestrial heat near Yeongduk and Ulsan, the analysis of crustal velocity anisotropy using the Pg phase indicates overall isotropy in the southern half of the Korean peninsula.

• Journal of Plant Biotechnology
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• v.33 no.1
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• pp.1-9
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• 2006

Peroxiredoxins (Prxs) are ubiquitously distributed and play important functions in diverse cellular signaling systems. The proteins are largely classified into three groups, such as typical 2-Cys Prx, atypical 2-Cys Prx, and 1-Cys Prx, that are distinguished by their catalytic mechanisms and number of Cys residues. From the three classes of Prxs, the typical 2-Cys Prx containing the two-conserved Cys residues at its N-terminus and C-terminus catalyzes $H_2O_2$ with the use of thioredoxin (Trx) as an electron donor. During the catalytic cycle, the N-terminal Cys residue undergoes a peroxide-dependent oxidation to sulfenic acid, which can be further oxidized to sulfinic acid at the presence of high concentrations of $H_2O_2$ and a Trx system containing Trx, Trx reductase, and NADPH. The sulfinic acid form of 2-Cys Prx is reduced by the action of sulfiredoxin which requires ATP as an energy source. Under the strong oxidative or heat shock stress conditions, 2-Cys Prx in eukaryotes rapidly switches its protein structure from low-molecular-weight species to high-molecular-weight protein structures. In accordance with its structural changes, the protein concomitantly triggers functional switching from a peroxidase to a molecular chaperone, which can protect its substrate denaturation from external stress. In addition to its N-terminal active site, the C-terminal domain including 'YF-motif' of 2-Cys Prx plays a critical role in the structural changes. Therefore, the C-terminal truncated 2-Cys Prxs are not able to regulate their protein structures and highly resistant to $H_2O_2$-dependent hyperoxidation, suggesting that the reaction is guided by the peroxidatic Cys residue. Based on the results, it may be concluded that the peroxidatic Cys of 2-Cys Prx acts as an '$H_2O_2$-sensor' in the cells. The oxidative stress-dependent regulation of 2-Cys Prx provides a means of defense systems in cells to adapt stress conditions by activating intracellular defense signaling pathways. Particularly, 2-Cys Prxs in plants are localized in chloroplasts with a dynamic protein structure. The protein undergoes conformational changes again oxidative stress. Depending on a redox-potential of the chloroplasts, the plant 2-Cys Prx forms super-molecular weight protein structures, which attach to the thylakoid membranes in a reversible manner.