TY  - JOUR
AU  - Nikodinović-Runić, Jasmina
AU  - Coulombel, Lydie
AU  - Francuski, Đorđe
AU  - Sharma, Narain D.
AU  - Boyd, Derek R.
AU  - Ferrall, Rory Moore O.
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1355
AB  - Nine different sulfur-containing compounds were biotransformed to the corresponding sulfoxides by Escherichia coli Bl21(DE3) cells expressing styrene monooxygenase (SMO) from Pseudomonas putida CA-3. Thioanisole was consumed at 83.3 mu moles min(-1) g cell dry weight(-1) resulting mainly in the formation of R-thioanisole sulfoxide with an enantiomeric excess (ee) value of 45 %. The rate of 2-methyl-, 2-chloro- and 2-bromo-thioanisole consumption was 2-fold lower than that of thioanisole. Surprisingly, the 2-methylthioanisole sulfoxide product had the opposite (S) configuration to that of the other 2-substituted thioanisole derivatives and had a higher ee value (84 %). The rate of oxidation of 4-substituted thioanisoles was higher than the corresponding 2-substituted substrates but the ee values of the products were consistently lower (10-23 %). The rate of benzo[b]thiophene and 2-methylbenzo[b]thiophene sulfoxidation was approximately 10-fold lower than that of thioanisole. The ee value of the benzo[b]thiophene sulfoxide could not be determined as the product racemized rapidly. E. coli cells expressing an engineered SMO (SMOeng R3-11) oxidised 2-substituted thioanisoles between 1.8- and 2.8-fold faster compared to cells expressing the wild-type enzyme. SMOeng R3-11 oxidised benzo[b]thiophene and 2-methylbenzo[b]thiophene 10.1 and 5.6 times faster that the wild-type enzyme. The stereospecificity of the reaction catalysed by SMOeng was unchanged from that of the wild type. Using the X-ray crystal structure of the P. putida S12 SMO, it was evident that the entrance of substrates into the SMO active site is limited by the binding pocket bottleneck formed by the side chains of Val-211 and Asn-46 carboxyamide group.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3
VL  - 97
IS  - 11
SP  - 4849
EP  - 4858
DO  - 10.1007/s00253-012-4332-5
ER  - 

@article{
author = "Nikodinović-Runić, Jasmina and Coulombel, Lydie and Francuski, Đorđe and Sharma, Narain D. and Boyd, Derek R. and Ferrall, Rory Moore O. and O'Connor, Kevin E.",
year = "2013",
abstract = "Nine different sulfur-containing compounds were biotransformed to the corresponding sulfoxides by Escherichia coli Bl21(DE3) cells expressing styrene monooxygenase (SMO) from Pseudomonas putida CA-3. Thioanisole was consumed at 83.3 mu moles min(-1) g cell dry weight(-1) resulting mainly in the formation of R-thioanisole sulfoxide with an enantiomeric excess (ee) value of 45 %. The rate of 2-methyl-, 2-chloro- and 2-bromo-thioanisole consumption was 2-fold lower than that of thioanisole. Surprisingly, the 2-methylthioanisole sulfoxide product had the opposite (S) configuration to that of the other 2-substituted thioanisole derivatives and had a higher ee value (84 %). The rate of oxidation of 4-substituted thioanisoles was higher than the corresponding 2-substituted substrates but the ee values of the products were consistently lower (10-23 %). The rate of benzo[b]thiophene and 2-methylbenzo[b]thiophene sulfoxidation was approximately 10-fold lower than that of thioanisole. The ee value of the benzo[b]thiophene sulfoxide could not be determined as the product racemized rapidly. E. coli cells expressing an engineered SMO (SMOeng R3-11) oxidised 2-substituted thioanisoles between 1.8- and 2.8-fold faster compared to cells expressing the wild-type enzyme. SMOeng R3-11 oxidised benzo[b]thiophene and 2-methylbenzo[b]thiophene 10.1 and 5.6 times faster that the wild-type enzyme. The stereospecificity of the reaction catalysed by SMOeng was unchanged from that of the wild type. Using the X-ray crystal structure of the P. putida S12 SMO, it was evident that the entrance of substrates into the SMO active site is limited by the binding pocket bottleneck formed by the side chains of Val-211 and Asn-46 carboxyamide group.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3",
volume = "97",
number = "11",
pages = "4849-4858",
doi = "10.1007/s00253-012-4332-5"
}

Nikodinović-Runić, J., Coulombel, L., Francuski, Đ., Sharma, N. D., Boyd, D. R., Ferrall, R. M. O.,& O'Connor, K. E.. (2013). The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3. in Applied Microbiology and Biotechnology
Springer, New York., 97(11), 4849-4858.
https://doi.org/10.1007/s00253-012-4332-5

Nikodinović-Runić J, Coulombel L, Francuski Đ, Sharma ND, Boyd DR, Ferrall RMO, O'Connor KE. The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3. in Applied Microbiology and Biotechnology. 2013;97(11):4849-4858.
doi:10.1007/s00253-012-4332-5 .

Nikodinović-Runić, Jasmina, Coulombel, Lydie, Francuski, Đorđe, Sharma, Narain D., Boyd, Derek R., Ferrall, Rory Moore O., O'Connor, Kevin E., "The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3" in Applied Microbiology and Biotechnology, 97, no. 11 (2013):4849-4858,
https://doi.org/10.1007/s00253-012-4332-5 . .

TY  - JOUR
AU  - Brooks, Sarah J.
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona
AU  - Doyle, Evelyn M.
AU  - O'Sullivan, Timothy
AU  - Guiry, Patrick J.
AU  - Coulombel, Lydie
AU  - Li, Zhi
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1352
AB  - 1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.
PB  - Springer, Dordrecht
T2  - Biotechnology Letters
T1  - Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase
VL  - 35
IS  - 5
SP  - 779
EP  - 783
DO  - 10.1007/s10529-013-1148-z
ER  - 

@article{
author = "Brooks, Sarah J. and Nikodinović-Runić, Jasmina and Martin, Leona and Doyle, Evelyn M. and O'Sullivan, Timothy and Guiry, Patrick J. and Coulombel, Lydie and Li, Zhi and O'Connor, Kevin E.",
year = "2013",
abstract = "1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.",
publisher = "Springer, Dordrecht",
journal = "Biotechnology Letters",
title = "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase",
volume = "35",
number = "5",
pages = "779-783",
doi = "10.1007/s10529-013-1148-z"
}

Brooks, S. J., Nikodinović-Runić, J., Martin, L., Doyle, E. M., O'Sullivan, T., Guiry, P. J., Coulombel, L., Li, Z.,& O'Connor, K. E.. (2013). Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters
Springer, Dordrecht., 35(5), 779-783.
https://doi.org/10.1007/s10529-013-1148-z

Brooks SJ, Nikodinović-Runić J, Martin L, Doyle EM, O'Sullivan T, Guiry PJ, Coulombel L, Li Z, O'Connor KE. Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters. 2013;35(5):779-783.
doi:10.1007/s10529-013-1148-z .

Brooks, Sarah J., Nikodinović-Runić, Jasmina, Martin, Leona, Doyle, Evelyn M., O'Sullivan, Timothy, Guiry, Patrick J., Coulombel, Lydie, Li, Zhi, O'Connor, Kevin E., "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase" in Biotechnology Letters, 35, no. 5 (2013):779-783,
https://doi.org/10.1007/s10529-013-1148-z . .

TY  - JOUR
AU  - Coulombel, Lydie
AU  - Nolan, Louise C.
AU  - Nikodinović-Runić, Jasmina
AU  - Doyle, Evelyn M.
AU  - O'Connor, Kevin E.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1161
AB  - Escherichia coli cells, expressing 4-hydroxyphenylacetate 3-hydroxylase, fully transformed 4-halogenated phenols to their equivalent catechols as single products in shaken flasks. 4-Fluorophenol was transformed at a rate 1.6, 1.8, and 3.4-fold higher than the biotransformation of 4-chloro-, 4-bromo-, and 4-iodo- phenol, respectively. A scale-up from shaken flask to a 5 L stirred tank bioreactor was undertaken to develop a bioprocess for the production of 4-substituted halocatechols at higher concentrations and scale. In a stirred tank reactor, the optimized conditions for induction of 4-HPA hydroxylase expression were at 37 C for 3 h. The rate of biotransformation of 4-fluorophenol to 4-fluorocatechol by stirred tank bioreactor grown cells was the same at 1 and 4.8 mM (5.13 mu mol/min/g CDW) once the ratio of biocatalyst (E. coli CDW) to substrate concentration (mM) was maintained at 2:1. At 10.8 mM 4-fluorophenol, the rate of 4-fluorocatechol formation decreased by 4.7-fold. However, the complete transformation of 1.3 g of 4-fluorophenol (10.8 mM) to 4-fluorocatechol was achieved within 7 h in a 1 L reaction volume. Similar to 4-fluorophenol, other 4-substituted halophenols were completely transformed to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM resulted in a 2.5-20-fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography resulted in the production of purified products with a final yield of between 33% and 38%.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase
VL  - 89
IS  - 6
SP  - 1867
EP  - 1875
DO  - 10.1007/s00253-010-2969-5
ER  - 

@article{
author = "Coulombel, Lydie and Nolan, Louise C. and Nikodinović-Runić, Jasmina and Doyle, Evelyn M. and O'Connor, Kevin E.",
year = "2011",
abstract = "Escherichia coli cells, expressing 4-hydroxyphenylacetate 3-hydroxylase, fully transformed 4-halogenated phenols to their equivalent catechols as single products in shaken flasks. 4-Fluorophenol was transformed at a rate 1.6, 1.8, and 3.4-fold higher than the biotransformation of 4-chloro-, 4-bromo-, and 4-iodo- phenol, respectively. A scale-up from shaken flask to a 5 L stirred tank bioreactor was undertaken to develop a bioprocess for the production of 4-substituted halocatechols at higher concentrations and scale. In a stirred tank reactor, the optimized conditions for induction of 4-HPA hydroxylase expression were at 37 C for 3 h. The rate of biotransformation of 4-fluorophenol to 4-fluorocatechol by stirred tank bioreactor grown cells was the same at 1 and 4.8 mM (5.13 mu mol/min/g CDW) once the ratio of biocatalyst (E. coli CDW) to substrate concentration (mM) was maintained at 2:1. At 10.8 mM 4-fluorophenol, the rate of 4-fluorocatechol formation decreased by 4.7-fold. However, the complete transformation of 1.3 g of 4-fluorophenol (10.8 mM) to 4-fluorocatechol was achieved within 7 h in a 1 L reaction volume. Similar to 4-fluorophenol, other 4-substituted halophenols were completely transformed to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM resulted in a 2.5-20-fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography resulted in the production of purified products with a final yield of between 33% and 38%.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase",
volume = "89",
number = "6",
pages = "1867-1875",
doi = "10.1007/s00253-010-2969-5"
}

Coulombel, L., Nolan, L. C., Nikodinović-Runić, J., Doyle, E. M.,& O'Connor, K. E.. (2011). Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. in Applied Microbiology and Biotechnology
Springer, New York., 89(6), 1867-1875.
https://doi.org/10.1007/s00253-010-2969-5

Coulombel L, Nolan LC, Nikodinović-Runić J, Doyle EM, O'Connor KE. Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. in Applied Microbiology and Biotechnology. 2011;89(6):1867-1875.
doi:10.1007/s00253-010-2969-5 .

Coulombel, Lydie, Nolan, Louise C., Nikodinović-Runić, Jasmina, Doyle, Evelyn M., O'Connor, Kevin E., "Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase" in Applied Microbiology and Biotechnology, 89, no. 6 (2011):1867-1875,
https://doi.org/10.1007/s00253-010-2969-5 . .