[1]冯琳琳,陈国涛,安雪姣,等.嗜热厌氧芽孢杆菌偶氮还原酶蛋白结构模拟分析及原核表达条件优化[J].应用与环境生物学报,2020,26(05):1251-1259.[doi: 10.19675/j.cnki.1006-687x.2019.10015]
　FENG Linlin,CHEN Guotao,AN Xuejiao,et al.Optimization of expression conditions and protein structure simulation analysis of azoreductase from Anoxybacillus sp.[J].Chinese Journal of Applied & Environmental Biology,2020,26(05):1251-1259.[doi: 10.19675/j.cnki.1006-687x.2019.10015]

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嗜热厌氧芽孢杆菌偶氮还原酶蛋白结构模拟分析及原核表达条件优化()

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1 郑洁. 生物法对偶氮染料废水脱色的研究[J]. 科技创新与应用, 2018, (32): 64-65 [Zheng J. A study of wastewater decolorization of azo dyes by biological method [J]. Technol Inno Appl, 2018 (32): 64-65]
2 孔春雷, 孙晓蕾, 周豪, 马桥, 张旭旺, 沈娥, 周集体, 曲媛媛. 菌株Acinetobacter sp. C-2对酸性红GR的脱色研究[J]. 环境科学与技术, 2013, 36 (3): 83-88 [Kong CL, Sun XL, Zhou H, Ma Q, Zhang XW, Shen E, Zhou JT, Qu YY. Biodecolorization of acid red GR by a newly isolated strain Acinetobacter sp. C-2 [J]. Environ Sci Technol, 2013, 36 (3): 83-88]
3 甘国娟, 田红灯, 潘永龙, Asit Mazumder, 潘响亮, 梁岩. 一株新的高效偶氮染料脱色菌Paenibacillus dendritiformis GGJ7及其脱色作用[J]. 应用与环境生物学报, 2018, 24 (3): 563-569 [Gan GJ, Tian HD, Pan YL, Asit M, Pan XL, Liang Y. A new efficient azo dye-decolorizing bacterium Paenibacillus dendritiformis GGJ7 and its decolorization process [J]. Chin J Appl Environ Biol, 2018, 24 (3): 563-569]
4 Mohamed SM, Mohamed KM, Samah AM, Neama AS, Mahmoud N. Bioremediation of red azo dye from aqueous solutions by a Spergillus niger strain isolated from textile wastewater [J]. J Environ Chem Eng, 2017, 5 (1): 547-554
5 Saraswathi VS, Neethu K, Bhaskara KV, Santhakumar K. Biofilm inhibition formation of clinical strains of Pseudomonas aeruginosa mutans, photocatalytic activity of azo dye and GC-MS analysis of leaves of Lagerstroemia speciosa [J]. J Photochem Photobiol B, 2017 (169): 148-160
6 Zimmermann T, Kulla HG, Leisinger T. Properties of purified orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46 [J]. Eur J Biochem, 1982, 129 (1): 197-203
7 Suzuki Y, Yoda T, Ruhul A, Sugiura W. Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil [J]. J Biol Chem, 2001, 276 (12): 9059-9065
8 Chen HZ, Wang RF, Cerniglia CE. Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis [J]. Protein Expr Purif, 2003, 34 (2): 302-310
9 Liger D, Graille M, Zhou CZ, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J, van Tilbeurgh H. Crystal structure and functional characterization of Yeast YLR011wp, an enzyme with NAD (P) H-FMN and Ferric Iron reductase activities [J]. J Biol Chem, 2004, 279 (33): 34890-34897
10 Liu ZJ, Chen HZ, Shaw N, L. Hopper S, Chen L, Chen S, E. Cerniglia C, Wang BCh. Crystal structure of an aerobic FMN-dependent azoreductase (AzoA) from Enterococcus faecalis [J]. Arch Biochem Biophys, 2007, 463 (1): 68-77
11 胡景华, 朱向东, 孔令保, 赖芬菊, 刘好桔, 陈浪, 张庆华. 一株嗜热偶氮染料脱色菌的分离鉴定及其脱色特性[J]. 环境工程学报, 2016, 10 (8): 4563-4568 [Hu JH, Zhu XD, Kong LB, Lai FJ, Liu HJ, Chen L, Zhang QH. Isolation and identification of a thermophilic azo dye decolorization bacterium and investigation of its decolorization characteristics [J]. Chin J Environ Eng, 2016, 10 (8): 4563-4568]
12 王国泽, 唐仁勇, 左福元, 郭秀兰, 陈康, 毛景欣. 瘤胃细菌DNA提取方法的研究与优化[J]. 黑龙江畜牧兽医, 2016 (16): 125-128 [Wang GZ, Tang RY, Zuo FY, Guo XL, Chen K, Mao JX. Study and optimization of DNA extraction method for rumen bacteria [J]. Heilongjiang Xumu Shouyi, 2016 (16): 125-128]
13 苏畅. 奥纳达希瓦氏菌重组表达偶氮还原酶及mtrA基因敲除研究[D]. 厦门: 厦门大学, 2017 [Su C. Recombinant expression of azoreductase and gene-knockout of mtrA on Shewanella oneidensis MR-1 [D]. Xiamen: Xiamen University, 2017]
14 Sigrid D, Sonja S, Rosemarie TE, Ilian J, Gübitz. Characterization of a thermostable NADPH: FMN oxidoreductase from the Mesophilic Bacterium Bacillus subtilis [J]. Biochemistry, 2006, 45 (23): 7083-7091
15 柳广飞. 偶氮还原酶AZR的结构模型与功能研究[D]. 大连: 大连理工大学, 2009 [Liu GF. Structure model and function of azoreductase AZR [D]. Dalian: Dalian University of Technology, 2009]
16 Cao XH, Di MX, Wang J. Expansion of the active site of the azoreductase from Shewanella oneidensis MR-1 [J]. J Mol GraphModell, 2017, 78 (17): 213-220
17 Nakanishi M, Yatome C, Ishida N, Kitade Y. Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase [J]. J Biol Chem, 2001, 276 (49): 46394-46399
18 ITO K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M. Crystal structure of azoreductase AzoR from Escherichia coli [J]. Proc Jpn Acad Ser B, 2005, 81 (6): 225-228
19 Morrison J. M, John GH. The non-enzymatic reduction of azo dyes by flavin and nicotinamide cofactors under varying conditions [J]. Anaerobe, 2013, (23): 87-96
20 Bürger S, Stolz A. Characterisation of the flavin-free oxygen-tolerant azoreductase from Xenophilus azovorans KF46F in comparison to flavin-containing azoreductases [J]. Appl Microbiol Biotechnol, 2010, 87 (6): 2067-2076
21 Ball J, Reis RAG, Agniswamy J, Weber IT, Gadda G. Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH: quinone oxidoreductase [J]. Protein Sci, 2019, 28: 167-175
22 Yu J, Ogata D, Gai ZQ, Taguchi S, Tanaka I, Ooi T, Yao M. Structures of AzrA and of AzrC complexed with substrate or inhibitor: insight into substrate specificity and catalytic mechanism [J]. Acta Crystallogr Sect D: Biol Crystallogr, 2014, 70 (5): 553-564
23 Feng J, Kweon O, Xu H, Cerniglia CE, Chen H. Probing the NADH- and Methyl Red-binding site of a FMN-dependent azoreductase (AzoA) from Enterococcus faecalis [J]. Arch Biochem Biophys, 2010, 520 (2): 99-107
24 Murataliev MB, Feyereisen R. Functional interactions in cytochrome P450BM3. evidence that NADP(H) binding controls redox potentials of the flavin cofactors [J]. Biochemistry, 2000, 39 (41): 12699-12707
25 Rakhi A, Jeffrey BB, Stephen KB, Subramanyam S. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal [J]. Acta Crystallogr Sect D: Biol Crystallogr, 2006, 62 (4): 383-391
26 Ito K, Nakanishi M, Lee WC, Zhi Y, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M. Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis [J]. J Biol Chem, 2008, 283 (20): 13889-13896
27 Ryan A, Laurieri N, Westwood I, Wang CJ, Lowe E, Sim E. A novel mechanism for azoreduction [J]. J Med Biosci Online, 2010, 400 (1): 24-37
28 Chazarreta-Cifre L, Martiarena L, de Mendoza D, Altabe SG. Role of ferredoxin and flavodoxins in Bacillus subtilis fatty acid desaturation [J]. J Bacteriol, 2011, 193 (16): 4043-4048
29 廖锡豪, 陈明祥, 谢万勇, 韩双艳, 林影. 低温诱导对毕赤酵母表达重组外源蛋白的影响[J]. 中国酿造, 2013, 32 (2): 9-12 [Liao XH, Chen MX, Xie WY, Han SY, Lin Y. Influence of low inducing temperature on foreign protein production in recombinant Pichia pastoris [J]. Chin Brew, 2013, 32 (2): 9-12]
30 Maryam E, Mohammad AA, Sedigheh A. Isolation, cloning and characterization of an azoreductase from the halophilic bacterium Halomonas elongata [J]. Int J Biol Macromol, 2016, 85: 111-116
31 许超, 黄桂媛, 王巧贞, 卢明倩, 张荣灿, 廖威, 张云开, 黄庶识. 褐藻胶裂解酶的基因克隆及表达条件优化[J]. 中国酿造, 2017, 36 (12): 120-125 [Xu C, Huang GY, Wang QZ, Lu MQ, Zhang RC, Liao W, Zhang YK, Huang SS. Conditions optimization of gene cloning and expression of alginate lyase [J]. Chin Brew, 2017, 36 (12): 120-125]
32 Kumar H, Nguyen QT, Binda C, Mattevi A, Fraaije MW. Isolation and characterization of a thermostable F420: NADPH oxidoreductase from Thermobifida fusca [J]. J Biol Chem, 2017, 292 (24): 10123-10130
33 Chang JS, Lin CY. Decolorization kinetics of a recombinant Escherichia coli strain harboring azo-dye-decolorizing determinants from Rhodococcus sp. [J]. Biotechnol Lett, 2001, 23 (8): 631-636