Multistep conversion of cresols by phenol hydroxylase and 2,3-dihydroxy-biphenyl 1,2-dioxygenase

详细信息    查看全文

• 作者：Shengnan Shi (1)
  Fang Ma (1)
  Tieheng Sun (1)
  Ang Li (1)
  Jiti Zhou (2)
  Yuanyuan Qu (2)
  
• 关键词：multistep conversion ; cresols ; phenol hydroxylase ; 2 ; 3 ; dihydroxybiphenyl 1 ; 2 ; dioxygenase ; methyl ; catechols
• 刊名：Frontiers of Environmental Science & Engineering
• 出版年：2014
• 出版时间：August 2014
• 年：2014
• 卷：8
• 期：4
• 页码：539-546
• 全文大小：
• 参考文献：1. Müller J A, Galushko A S, Kappler A, Schink B. Anaerobic degradation of / m-cresol by / Desulfobacterium cetonicum is initiated by formation of 3-hydroxybenzylsuccinate. Archives of Microbiology, 1999, 172(5): 287-94 CrossRef
  2. Londry K L, Fedorak PM, Suflita J M. Anaerobic degradation of / m-Cresol by a sulfate-reducing bacterium. Applied and Environmental Microbiology, 1997, 63(8): 3170-175
  3. Tallur P N, Megadi V B, Kamanavalli C M, Ninnekar H Z. Biodegradation of / p-cresol by / Bacillus sp. strain PHN 1. Current Microbiology, 2006, 53(6): 529-33 CrossRef
  4. Knackmuss H J. Biochemistry and practical implications of organohalide degradation. In: Klug M J, Reddy C A, eds. Current Perspectives in Microbial. Washington, D C: American Society for Microbiology, 1984, 687-93
  5. Dagley S, Gibson D T. The bacterial degradation of catechol. The Biochemical Journal, 1965, 95(2): 466-74
  6. Coulombel L, Nolan L C, Nikodinovic J, Doyle E M, O’Connor K E. Biotransformation of 4-halophenols to 4-halocatechols using / Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. Applied Microbiology and Biotechnology, 2011, 89(6): 1867-875 CrossRef
  7. Qu Y Y, Shi S N, Qiao M, Kong C L, Zhou H, Zhang X W, Zhou J T. Multistep conversion of / para-substituted phenols by phenol hydroxylase and 2,3-dihydroxy-biphenyl 1,2-dioxygenase. Applied Biochemistry and Biotechnology, 2013, 169(7): 2064-075. CrossRef
  8. Tao Y, Fishman A, Bentley W E, Wood T K. Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by toluene 4-monooxygenase of / Pseudomonas mendocina KR1 and toluene 3-monooxygenase of / Ralstonia pickettii PKO1. Applied and Environmental Microbiology, 2004, 70(7): 3814-820 CrossRef
  9. Roberts S J, Morris J C, Dobson R C J, Gerrard J A. The preparation of (S)-aspartate semi-aldehyde appropriate for use in biochemical studies. Bioorganic & Medicinal Chemistry Letters, 2003, 13(2): 265-67 CrossRef
  10. Parales R E, Bruce N C, Schmid A, Wackett L P. Biodegradation, biotransformation, and biocatalysis (b3). Applied and Environmental Microbiology, 2002, 68(10): 4699-709 CrossRef
  11. Garikipati S V, McIver A M, Peeples T L. Whole-cell biocatalysis for 1-naphthol production in liquid-liquid biphasic systems. Applied and Environmental Microbiology, 2009, 75(20): 6545-552 CrossRef
  12. Pollard D J, Woodley J M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends in Biotechnology, 2007, 25(2): 66-3 CrossRef
  13. Schmid A, Dordick J S, Hauer B, Kiener A, Wubbolts M, Witholt B. Industrial biocatalysis today and tomorrow. Nature, 2001, 409(6817): 258-68 CrossRef
  14. Azerad R. Editorial overview: better enzyme for green chemistry. Current Opinion in Biotechnology, 2001, 12(6): 533-34 CrossRef
  15. Straathof A J J, Panke S, Schmid A. The production of fine chemicals by biotransformations. Current Opinion in Biotechnology, 2002, 13(6): 548-56 CrossRef
  16. Selinheimo E, Gasparetti C, Mattinen M L, Steffensen C L, Buchert J, Kruus K. Comparison of substrate specificity of tyrosinases from / Trichoderma reesei and / Agaricus bisporus. Enzyme and Microbial Technology, 2009, 44(1): 1-0
  17. Sazinsky M H, Dunten P W, McCormick M S, DiDonato A, Lippard S J. X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, / Pseudomonas sp. OX1 phenol hydroxylase. Biochemistry, 2006, 45(51): 15392-5404 CrossRef
  18. Eltis L D, Hofmann B, Hecht H J, Lünsdorf H, Timmis K N. Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase. The Journal of Biological Chemistry, 1993, 268(4): 2727-732
  19. Wu Z L, Podust L M, Guengerich F P. Expansion of substrate specificity of cytochrome P450 2A6 by random and site-directed mutagenesis. The Journal of Biological Chemistry, 2005, 280(49): 41090-1100 CrossRef
  20. Morris G M, Lim-Wilby M. Molecular docking. Methods in Molecular Biology (Clifton, N.J.), 2008, 443(1064-745): 365-82 CrossRef
  21. Ma F, Shi S N, Sun T H, Li A, Zhou J T, Qu Y Y. Biotransformation of benzene and toluene to catechols by phenol hydroxylase from / Arthrobacter sp. W1. Applied Microbiology and Biotechnology, 2013, 97(11): 5097-103 CrossRef
  22. Carliell CM, Barclay S J, Naidoo N, Buckley C A, Mulholland D A, Senior E. Microbial decolorization of a reactive azo dye under anaerobic conditions. Water SA, 1995, 21(1): 61-9
  
• 作者单位：Shengnan Shi (1)
  Fang Ma (1)
  Tieheng Sun (1)
  Ang Li (1)
  Jiti Zhou (2)
  Yuanyuan Qu (2)
  
  1. State Key Laboratory of Urban Water Resource and Environment, School of Municipal and Environmental Engineering, Harbin Institute of Technology, Harbin, 150090, China
  2. Key Laboratory of Industrial Ecology and Environmental Engineering (Ministry of Education), School of Environmental Science and Technology, Dalian University of Technology, Dalian, 116024, China
  
• ISSN：2095-221X

文摘

A multistep conversion system composed of phenol hydroxylase (PHIND) and 2,3-dihydroxy-biphenyl 1,2-dioxygenase (BphCLA-4) was used to synthesize methylcatechols and semialdehydes from o- and m-cresol for the first time. Docking studies displayed by PyMOL predicted that cresols and methylcatechols could be theoretically transformed by this multistep conversion system. High performance liquid chromatography mass spectrometry (HPLC-MS) analysis also indicated that the products formed from multistep conversion were the corresponding 3-methylcatechol, 4-methylcatechol, 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoic acid (2-hydroxy-3-methyl-ODA) and 2-hydroxy-5-methyl-6-oxohexa-2,4-dienoic acid (2-hydroxy-5-methyl-ODA). The optimal cell concentrations of the recombinant E. coli strain BL21 (DE3) expressing phenol hydroxylase (PHIND) and 2,3-dihydroxy-biphenyl 1,2-dioxygenase (BphCLA-4) and pH for the multistep conversion of o- and m-cresol were 4.0 (g·L? cell dry weight) and pH 8.0, respectively. For the first step conversion, the formation rate of 3-methylcatechol (0.29 μmol·L?·min?·mg? cell dry weight) from o-cresol was similarly with that of methylcatechols (0.28 μmol·L?·min?·mg? cell dry weight) from m-cresol by strain PHIND. For the second step conversion, strain BphCLA-4 showed higher formation rate (0.83 μmol ·L?·min?·mg? cell dry weight) for 2-hydroxy-3-methyl-ODA and 2-hydroxy-5-methyl-ODA from m-cresol, which was 1.1-fold higher than that for 2-hydroxy-3-methyl-ODA (0.77 μmol·L?·min?·mg?cell dry weight) from o-cresol. The present study suggested the potential application of the multistep conversion system for the production of chemical synthons and high-value products.