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题名: pH-induced quaternary assembly of Vitreoscilla hemoglobin: The monomer exhibits better peroxidase activity
作者: Li, Wei1;  Zhang, Yubin1, 4;  Xu, Haoran1;  Wu, Lei3;  Cao, Yufeng5;  Zhao, Haifeng6;  Li, Zhengqiang1, 2
关键词: Vitreoscilla hemoglobin ;  Peroxidase activity ;  Dimer-monomer-dimer transition
刊名: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
发表日期: 2013-10-01
DOI: 10.1016/j.bbapap.2013.07.005
卷: 1834, 期:10, 页:2124-2132
收录类别: SCI
文章类型: Article
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
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.
关键词[WOS]: RELIEVES NITROSATIVE STRESS ;  BACTERIAL GLOBIN GENE ;  ESCHERICHIA-COLI ;  CYTOCHROME-O ;  OXYGEN-BINDING ;  EXPRESSION ;  GROWTH ;  PURIFICATION ;  REDUCTASE ;  RIBOSOME
语种: 英语
WOS记录号: WOS:000325236700019
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/137563
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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

Recommended Citation:
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.
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