KOPRI Repository

Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica

Cited 0 time in scopus
Metadata Downloads
Title
Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica
Other Titles
벼에 존재하는 산화된 비타민의 환원 및 재생에 관여하는 DHAR 효소의 구조 및 기능 연구
Authors
Hackwon Do
Lee, Jun Hyuck
Kim, Han-Woo
Yoon, Ho-Sung
Young-Saeng Kim
Park, Hyun
Shin, Seung Chul
Wi, Ah Ram
Park, Ae Kyung
Lee, Chang Woo
Byoung Wook Jeon
Il-Sup Kim
Keywords
Oryza sativa L. japonica; X-ray crystallography; ascorbate; dehydroascorbate reductase
Issue Date
2016
Citation
Hackwon Do, et al. 2016. "Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica". SCIENTIFIC REPORTS, 6(19498): 1-13.
Abstract
Dehydroascorbate reductase (DHAR) is a key enzyme involved in the recycling of ascorbate, which catalyses the glutathione (GSH)-dependent reduction of oxidized ascorbate (dehydroascorbate, DHA). As a result, DHAR regenerates a pool of reduced ascorbate and detoxifies reactive oxygen species (ROS). In previous experiments involving transgenic rice, we observed that overexpression of DHAR enhanced grain yield and biomass. Since the structure of DHAR is not available, the enzymatic mechanism is not well-understood and remains poorly characterized. To elucidate the molecular basis of DHAR catalysis, we determined the crystal structures of DHAR from Oryza sativa L. japonica (OsDHAR) in the native, ascorbate-bound, and GSH-bound forms and refined their resolutions to 1.9, 1.7, and 1.7 A, respectively. These complex structures provide the first information regarding the location of the ascorbate and GSH binding sites and their interacting residues. The location of the ascorbate-binding site overlaps with the GSH-binding site, suggesting a ping-pong kinetic mechanism for electron transfer at the common Cys20 active site. Our structural information and mutagenesis data provide useful insights into the reaction mechanism of OsDHAR against ROS-induced oxidative stress in rice.
URI
http://repository.kopri.re.kr/handle/201206/7427
DOI
http://dx.doi.org/doi:10.1038/srep19498
Files in This Item
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    qrcode

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

    Browse