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Open AccessArticle

Characterization and Structural Determination of Cold-Adapted Monodehydroascorbate Reductase, MDHAR, from the Antarctic Hairgrass Deschampsia Antarctica

1
Unit of Research for Practical Application, Korea Polar Research Institute, Incheon 21990, Korea
2
Division of Bacterial Diseases, Center for Laboratory Control of Infectious Diseases, Korea Centers for Diseases Control and Prevention, Chungcheongbuk-do 28159, Korea
3
Advanced Bioresource Research Center, Kyungpook National University, Daegu 41566, Korea
4
Department of Pathology and Genomic Medicine, Houston Methodist Hospital Research Institute, Houston, TX 77030, USA
5
Department of Energy Science, Kyungpook National University, Daegu 41566, Korea
6
Department of Polar Sciences, University of Science and Technology, Incheon 21990, Korea
7
School of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Korea
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Crystals 2019, 9(10), 537; https://doi.org/10.3390/cryst9100537
Received: 18 September 2019 / Revised: 16 October 2019 / Accepted: 17 October 2019 / Published: 18 October 2019
(This article belongs to the Special Issue Crystallographic Studies of Enzymes)
Ascorbic acid (AsA) is an abundant component of plants and acts as a strong and active antioxidant. In order to maintain the antioxidative capacity of AsA, the rapid regeneration of AsA is regulated by dehydroascorbate reductase (DHAR) and monodehydroascorbate reductase (MDHAR). To understand how MDHAR functions under extreme temperature conditions, this study characterized its biochemical properties and determined the crystal structure of MDHAR from the Antarctic hairgrass Deschampsia antarctica (DaMDHAR) at 2.2 Å resolution. This allowed for a structural comparison with the mesophilic MDHAR from Oryza sativa L. japonica (OsMDHAR). In the functional analysis, yeast cells expressing DaMDHAR were tolerant to freezing and thawing cycles. It is possible that the expression of DaMDHAR in yeast enhanced the tolerance for ROS-induced abiotic stress. View Full-Text
Keywords: monodehydroascorbate reductase; Antarctic hairgrass; cold adaptation monodehydroascorbate reductase; Antarctic hairgrass; cold adaptation
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MDPI and ACS Style

Park, A.K.; Kim, I.-S.; Do, H.; Kim, H.; Choi, W.; Jo, S.-W.; Shin, S.C.; Lee, J.H.; Yoon, H.-S.; Kim, H.-W. Characterization and Structural Determination of Cold-Adapted Monodehydroascorbate Reductase, MDHAR, from the Antarctic Hairgrass Deschampsia Antarctica. Crystals 2019, 9, 537. https://doi.org/10.3390/cryst9100537

AMA Style

Park AK, Kim I-S, Do H, Kim H, Choi W, Jo S-W, Shin SC, Lee JH, Yoon H-S, Kim H-W. Characterization and Structural Determination of Cold-Adapted Monodehydroascorbate Reductase, MDHAR, from the Antarctic Hairgrass Deschampsia Antarctica. Crystals. 2019; 9(10):537. https://doi.org/10.3390/cryst9100537

Chicago/Turabian Style

Park, Ae K.; Kim, Il-Sup; Do, Hackwon; Kim, Hyun; Choi, Woong; Jo, Seung-Woo; Shin, Seung C.; Lee, Jun H.; Yoon, Ho-Sung; Kim, Han-Woo. 2019. "Characterization and Structural Determination of Cold-Adapted Monodehydroascorbate Reductase, MDHAR, from the Antarctic Hairgrass Deschampsia Antarctica" Crystals 9, no. 10: 537. https://doi.org/10.3390/cryst9100537

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