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Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase
You, Cai1,2,3; Liu, Changshui1,2; Li, Yingjie1,2; Jiang, Peng1,2; Ma, Qingjun1,2
2018-05-01
Source PublicationINTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN0141-8130
Volume111Pages:1175-1182
Corresponding AuthorJiang, Peng(jiangpeng@qdio.ac.cn) ; Ma, Qingjun(qma@qdio.ac.cn)
AbstractRapid accumulations of unattached green macroalgae, referred to as blooms, constitute ecological disasters and occur in many coastal regions. Ulva are a major cause of blooms, owing to their high nitrogen utilization capacity, which requires nitrate reductase (NR) activity; however, molecular characterization of Ulva NR remains lacking. Herein we determined the crystal structure and performed an enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera NR (UpCbRNR). The structural analysis revealed an N-terminal FAD-binding domain primarily consisting of six antiparallel beta strands, a C-terminal NADH-binding domain forming a Rossmann fold, and a three beta-stranded linker region connecting these two domains. The FAD cofactor was located in the cleft between the two domains and interacted primarily with the FAD-binding domain. UpCbRNR shares similarities in overall structure and cofactor interactions with homologs, and its catalytic ability is comparable to that of higher plant CbRNRs. Structure and sequence comparisons of homologs revealed two regions of sequence length variation potentially useful for phylogenetic analysis: one in the FAD-binding domain, specific to U. prolifera, and another in the linker region that may be used to differentiate between plant, fungi, and animal homologs. Our data will facilitate molecular-level understanding of nitrate assimilation in Ulva. (C) 2018 Elsevier B.V. All rights reserved.
KeywordUlva prolifera Nitrate reductase Indel Cytochrome b(5) reductase
DOI10.1016/j.ijbiomac.2018.01.140
Indexed BySCI
Language英语
Funding Project1000 Talents Program of China ; 100 Talents Program of the Chinese Academy of Sciences ; AoShan Talents Program of Qingdao National Laboratory for Marine Science and Technology[2015ASTP]
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry ; Polymer Science
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Applied ; Polymer Science
WOS IDWOS:000429391000133
PublisherELSEVIER SCIENCE BV
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/158656
Collection实验海洋生物学重点实验室
Corresponding AuthorJiang, Peng; Ma, Qingjun
Affiliation1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Nanhai Rd 7, Qingdao 266071, Peoples R China
2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
First Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Corresponding Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
GB/T 7714
You, Cai,Liu, Changshui,Li, Yingjie,et al. Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2018,111:1175-1182.
APA You, Cai,Liu, Changshui,Li, Yingjie,Jiang, Peng,&Ma, Qingjun.(2018).Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,111,1175-1182.
MLA You, Cai,et al."Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 111(2018):1175-1182.
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