中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase

文献类型:期刊论文

作者You, Cai1,2,3; Liu, Changshui1,2; Li, Yingjie1,2; Jiang, Peng1,2; Ma, Qingjun1,2
刊名INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
出版日期2018-05-01
卷号111页码:1175-1182
关键词Ulva prolifera Nitrate reductase Indel Cytochrome b(5) reductase
ISSN号0141-8130
DOI10.1016/j.ijbiomac.2018.01.140
通讯作者Jiang, Peng(jiangpeng@qdio.ac.cn) ; Ma, Qingjun(qma@qdio.ac.cn)
英文摘要Rapid 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.
资助项目1000 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研究方向Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
语种英语
WOS记录号WOS:000429391000133
出版者ELSEVIER SCIENCE BV
源URL[http://ir.qdio.ac.cn/handle/337002/158655]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Jiang, Peng; Ma, Qingjun
作者单位1.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
推荐引用方式
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.

入库方式: OAI收割

来源:海洋研究所

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