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Review Article
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doi:10.4172/2155-6199.1000112
Environmental Biotechnology, Microbial Type Culture Collection and Gene Bank (MTCC), Institute of Microbial Technology, Sector-39A, Chandigarh-160036, India
Department of Plant Science, Faculty of Applied Sciences, M.J.P. Rohilkhand University, Bareilly -243006, India
Abstract
Monooxygenases act as biocatalysts in bioremediation process and synthetic chemistry due to their highly
regioselectivity and sterioselectivity on wide range of substrates. They are involved in the process of desulfurization,
dehalogenation, denitrification, ammonification, hydroxylation, biotransformation and biodegradation of various aromatic
and aliphatic compounds. In the recent years, the practical applications of monooxygenases have been improved using
the approaches of directed evolution, meta-genomics and bioinformatics. This review is focused on current applications
of monooxygenses especially in biodegradation and biotransformation of aromatic compounds.
Introduction
Aromatic compounds are persistence environmental pollutants
that are widely distributed in the biosphere due to anthropogenic
activities. These compounds are highly toxic to living beings; therefore,
many of them have been listed as priority pollutants by United
States Environmental Protection Agency. Microbial degradation has
emerged as an effective technology to remove these compounds
from environment. Many microbial enzymes such as oxygenases,
dehalogenases, reductases, hydroxylases and dehydrogenases are
involved in the degradation of these environmental pollutants. Among
them, oxygenases are the key enzymes for aerobic biodegradation
of aromatic compounds because they are involved in the initial
reaction of degradation and also catalyze the ring cleavage of the
aromatic compounds which is the essential step for the complete
mineralization of these compounds [1].
monooxygenase (TcmH) from Streptomyces glauscens [5]; ActVAorf6 monooxygenase from Streptomycescoelicolor A3(2) [6]; quinol
monooxygenase (YgiN) from E. Coli [7] and Rv0793 a hypothetical
monooxygenase from Mycobacteriumtuberculosis [8].
Aromatic dioxygenase are also divided into two subclasses
based on mode of action: aromatic ring hydroxylation dioxygenases
(ARHDs) and aromatic ring cleavage dioxygenases (ARCDs) [1]. ARHD
catalyzes the incorporation of both atoms of oxygen into aromatic
ring (Figure 1b) whereas ARCD catalyzes ring cleavage of the aromatic
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
Page 2 of 8
ring typically carrying two or more hydroxyl groups [1]. ARCDs are
further divided into two groups based on the ring cleavage: intradiol
(IARCD) and extradiol (EARCD) [1]. Intradiol cleaves the aromatic ring
between two hydroxyl groups (ortho-cleavage) (Figure 1c), whereas
extradiol cleaves the aromatic ring between a hydroxylated carbon
and an adjacent non-hydroxylated carbon (meta-cleavage) (Figure 1d).
Several publications have been focused on dioxygenases and
their role in biodegradation [9-12]. But very few reviews are available
that cover the role of the monooxygenases in biodegradation
[13]. In this review, we have discussed the current applications of
the monooxygenases in biodegradation and biotransformation of
aromatic compounds.
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
Page 3 of 8
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
Page 4 of 8
were transformed all DBT into 50% mixture of HBPS and HBP [51]. In
the second step, the cells of late exponential phase have removed
and the early exponential phase cells (5 h grown cells) were added.
After addition remaining HBPS was efficiently converted to HBP [51].
Another recombinant bacteria has been design by transferring
the pVLT31 vector harboring flavin-oxidoreductase gene (dszD) into
the recombinant P. aeruginosa ATCC 9027 which contained dszABC
gene in its chromosome stably [52]. This recombinant bacteria
showed the enhanced activity of biodesulfurization when all four
genes co expressed. The biodesulfurization efficiency has also been
significantly improved using the approach of directed evolution.
Arensdorf et al. (2002) presented an example of directed evolution
of biodesulfurization using chemostat approach [53]. Rhodococcus
erythropolis IGTS8 has not ability to utilize octyl sulphide and
5-methylbenzothiophene (5-MBT) as sole sulphur sources. Arensdorf
et al. (2002) selected gain-of-function mutants of strain IGTS8 using
sulphur limited chemostat [53]. These mutants were grown with octyl
sulphide and 5-MBT as sole sulphur sources. The ability of mutant
to grow on 5-MBT as sole sulphur source was due to a transversion
(guanine to thymine) in dszC codon 261 [53].
Enzyme
E.C number
Substrate(s)
References
1.13.12.-
4-Methyl-5-nitrocatechol
[58]
Toluene 3-monooxygenase
1.14.-.-
3-Hydroxytoluene, Toluene
[59]
Toluene 2-monooxygenase
1.14.13.-
4-Hydroxyacetophenone monooxygenase
1.14.13.-
4-Hydroxyacetophenone
[61]
Toluene 4-monooxygenase
1.14.13.-
Toluene, N-Nitrosodimethylamine
[62]
4-Hydroxybenzoate 3-monooxygenase
1.14.13.2
4-Hydroxybenzoate
[63]
2-Mercaptobenzothiazole monooxygenase
http://umbbd.msi.umn.edu/servlets/
pageservlet?ptype=r&reacID=r1178 1.14.-.-
2-Mercaptobenzothiazole
[64]
6-Hydroxy-2-mercaptobenzothiazole
monooxygenase
1.14.-.-
6-Hydroxy-2-mercaptobenzothiazole
[64]
Benzothiazole monooxygenase
1.14.-.-
Benzothiazole
[65]
1.14.-.-
Phenylboronic acid
[66]
2,6-Dihydroxybenzothiazole monooxygenase
1.14.-.-
2,6-Dihydroxybenzothiazole
[67]
2-Hydroxybenzothiazole monooxygenase
1.14.-.-
2-Hydroxybenzothiazole
[65]
1-Indanone monooxygenase
1.14.-.-
1-Indanone
[68]
2-Indanone monooxygenase
1.14.-.-
2-Indanone
[68]
6-Hydroxy-3-methyl-2-oxo-1,2-dihydroquinoline
6-monooxygenase
1.14.-.-
6-Hydroxy-3-methyl-2-oxo-1,2-dihydroquinoline
[69]
Toluene-4-sulfonate monooxygenase
1.14.-.-
Toluene 4-sulfonate
[70]
1.14.13.-
Dibenzothiophene-5,5-dioxide
[71]
1.14.-.-
3-Methyl-2-oxo-1,2-dihydroquinoline
[69]
BCDS monooxygenase
1.14.-.-
[72]
1.14.13.-
Toluene-4-sulfonate
[73]
Orcinol 2-monooxygenase
1.14.13.6
Orcinol
[74]
3-Hydroxybenzoate 4-hydroxylase
1.14.13.23
3-Hydroxybenzoate
[75]
3-Hydroxybenzoate 6-monooxygenase
1.14.13.24
3-Hydroxybenzoate
[76]
4-Methoxybenzoate monooxygenase
1.14.99.15
4-methoxybenzoate
[77]
Benzoate 4-monooxygenase
1.14.13.12
Benzoate
[78]
N-isopropylacetaniline monooxygenase
1.14.15.-
N-Isopropylacetanilide
[79]
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
Page 5 of 8
Phenylacetone monooxygenase (PAMO, EC 1.14.13.92) is a FADcontaining Baeyer-Villiger monooxygenase (BVMO). This enzyme was
discovered from Thermobifida fusca that is a moderately thermophilic
soil bacterium and grows at 55C. PAMO oxidizes phenylacetone,
aromatic and aliphatic ketones, aromatic sulphides and sulphoxides
and organoborn compounds [87]. This enzyme has thermostability
and tolerance towards organic solvents [88], therefore, this enzyme
is suitable for various industrial applications.
Conclusion
Monooxygenases are multifunctional enzymes and involved in
biodesulfurization, dehalogenation, denitrification and hydroxylation
of various aromatic compounds. The applications of monooxygenases
have been improved using the recent molecular and bioinformatic
approaches.
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
Page 6 of 8
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
Page 7 of 8
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Citation: Arora PK, Srivastava A, Singh VP (2010) Application of Monooxygenases in Dehalogenation, Desulphurization, Denitrification and
Hydroxylation of Aromatic Compounds. J Bioremed Biodegrad 1:112. doi:10.4172/2155-6199.1000112
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