Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase

doi:10.1016/j.ijbiomac.2018.01.140

CORC > 海洋研究所 > 中国科学院海洋研究所 > 实验海洋生物学重点实验室

	Structural and enzymatic analysis of the cytochrome b(5) reductase domain of Ulva prolifera nitrate reductase
	You, Cai 1,2,3; Liu, Changshui 1,2; Li, Yingjie 1,2; Jiang, Peng 1,2; Ma, Qingjun 1,2
刊名	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
	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
DOI	10.1016/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
出版者	ELSEVIER SCIENCE BV
WOS记录号	WOS:000429391000133
内容类型	期刊论文
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.