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Park AK, Kim IS, Do H, et al. Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica. Sci Rep. 2016;6:33903doi: 10.1038/srep33903.
Park, A. K., Kim, I. S., Do, H., Jeon, B. W., Lee, C. W., Roh, S. J., Shin, S. C., Park, H., Kim, Y. S., Kim, Y. H., Yoon, H. S., Lee, J. H., & Kim, H. W. (2016). Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica. Scientific reports, 633903. https://doi.org/10.1038/srep33903
Park, Ae Kyung, et al. "Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica." Scientific reports vol. 6 (2016): 33903. doi: https://doi.org/10.1038/srep33903
Park AK, Kim IS, Do H, Jeon BW, Lee CW, Roh SJ, Shin SC, Park H, Kim YS, Kim YH, Yoon HS, Lee JH, Kim HW. Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica. Sci Rep. 2016 Sep 22;6:33903. doi: 10.1038/srep33903. PMID: 27652777; PMCID: PMC5031999.
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Sci Rep. 2016 Sep 22;6:33903. doi: 10.1038/srep33903.

Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica.

Scientific reports

Ae Kyung Park, Il-Sup Kim, Hackwon Do, Byung Wook Jeon, Chang Woo Lee, Soo Jung Roh, Seung Chul Shin, Hyun Park, Young-Saeng Kim, Yul-Ho Kim, Ho-Sung Yoon, Jun Hyuck Lee, Han-Woo Kim

Affiliations

  1. Division of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
  2. School of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea.
  3. Department of Polar Sciences, University of Science and Technology, Incheon 21990, Republic of Korea.
  4. Research Institute for Ulleung-do &Dok-do, Kyungpook National University, Daegu 41566, Republic of Korea.
  5. Highland Agriculture Research Institute, National Institute of Crop Science, Rural Development Administration, Pyeongchang 25342, Republic of Korea.

PMID: 27652777 PMCID: PMC5031999 DOI: 10.1038/srep33903

Abstract

Ascorbic acid (AsA) maintains redox homeostasis by scavenging reactive oxygen species from prokaryotes to eukaryotes, especially plants. The enzyme monodehydroascorbate reductase (MDHAR) regenerates AsA by catalysing the reduction of monodehydroascorbate, using NADH or NADPH as an electron donor. The detailed recycling mechanism of MDHAR remains unclear due to lack of structural information. Here, we present the crystal structures of MDHAR in the presence of cofactors, nicotinamide adenine dinucleotide (NAD

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