中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
pH-induced quaternary assembly of Vitreoscilla hemoglobin: The monomer exhibits better peroxidase activity

文献类型:期刊论文

作者Li, Wei1; Zhang, Yubin1,4; Xu, Haoran1; Wu, Lei3; Cao, Yufeng5; Zhao, Haifeng6; Li, Zhengqiang1,2
刊名biochimica et biophysica acta-proteins and proteomics
出版日期2013-10-01
卷号1834期号:10页码:2124-2132
关键词Vitreoscilla hemoglobin Peroxidase activity Dimer-monomer-dimer transition
英文摘要ph-dependent (ph 6.0-8.0) quaternary structural changes of ferric vitreoscilla hemoglobin (vhb) have been investigated using dynamic light scattering. the vhb exhibits a monomeric state under neutral conditions at ph 7.0, while the protein forms distinct homodimeric species at ph 6.0 and 8.0, respectively. the dissociation constant obtained using the bio-layer interferometry technology indicates that, at ph 7.0, the monomer-monomer dissociation of vhb is about 6-fold or 5-fold higher (k-d = 634 mu m) compared with that at slightly acidic ph (k-d = 1.05 mu m) or slightly alkaline ph (k-d = 1.22 mu m). the ph-dependent absorption spectra demonstrate that the heme microenvironment of vhb is sensitive to the changes of ph value. the maximum absorption band of heme group of vhb shifts from 402 nm to 407 nm when ph changes from 6.0 to 8.0. in addition, the fluorescence emission spectra of vhb, taken at excitation wavelength of 295 nm, suggest that the single trp122 fluorescence quantum yields in vhb are decreased due to the formation of the homodimeric species. however, the circular dichroism spectra data display that the secondary structures of vhb are little affected by ph transitions. the ph-dependent peroxidase activity of vhb was also investigated in this study. the optimum ph for vhb using 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) as substrate is 7.0, which implies that the monomer state of vhb would exhibit better peroxidase activity than the homodimeric species of vhb at ph 6.0 and 8.0. (c) 2013 elsevier b.v. all rights reserved.
WOS标题词science & technology ; life sciences & biomedicine
类目[WOS]biochemistry & molecular biology ; biophysics
研究领域[WOS]biochemistry & molecular biology ; biophysics
关键词[WOS]relieves nitrosative stress ; bacterial globin gene ; escherichia-coli ; cytochrome-o ; oxygen-binding ; expression ; growth ; purification ; reductase ; ribosome
收录类别SCI
语种英语
WOS记录号WOS:000325236700019
公开日期2015-11-10
源URL[http://159.226.238.44/handle/321008/137563]  
专题大连化学物理研究所_中国科学院大连化学物理研究所
作者单位1.Jilin Univ, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130012, Peoples R China
2.Jilin Univ, Sch Life Sci, Changchun 130012, Peoples R China
3.Jilin Agr Univ, Coll Life Sci, Changchun 130018, Peoples R China
4.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, Beijing 100864, Peoples R China
5.Changchun Med Coll, Fundamental Nursing Dept, Changchun 130031, Peoples R China
6.Jilin Inst Food & Drug Control, Changchun 130000, Peoples R China
推荐引用方式
GB/T 7714
Li, Wei,Zhang, Yubin,Xu, Haoran,et al. pH-induced quaternary assembly of Vitreoscilla hemoglobin: The monomer exhibits better peroxidase activity[J]. biochimica et biophysica acta-proteins and proteomics,2013,1834(10):2124-2132.
APA Li, Wei.,Zhang, Yubin.,Xu, Haoran.,Wu, Lei.,Cao, Yufeng.,...&Li, Zhengqiang.(2013).pH-induced quaternary assembly of Vitreoscilla hemoglobin: The monomer exhibits better peroxidase activity.biochimica et biophysica acta-proteins and proteomics,1834(10),2124-2132.
MLA Li, Wei,et al."pH-induced quaternary assembly of Vitreoscilla hemoglobin: The monomer exhibits better peroxidase activity".biochimica et biophysica acta-proteins and proteomics 1834.10(2013):2124-2132.

入库方式: OAI收割

来源:大连化学物理研究所

浏览0
下载0
收藏0
其他版本

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。