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  - Boyd, Derek R.
AU  - Sharma, Narain D.
AU  - McMurray, Brian
AU  - Haughey, Simon A.
AU  - Allen, Christopher C. R.
AU  - Hamilton, John T. G.
AU  - McRoberts, W. Colin
AU  - O'Ferrall, Rory A. More
AU  - Nikodinović-Runić, Jasmina
AU  - Coulombel, Lydie A.
AU  - O'Connor, Kevin E.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1238
AB  - Asymmetric heteroatom oxidation of benzo[b]thiophenes to yield the corresponding sulfoxides was catalysed by toluene dioxygenase (TDO), naphthalene dioxygenase (NDO) and styrene monooxygenase (SMO) enzymes present in P. putida mutant and E. coli recombinant whole cells. TDO-catalysed oxidation yielded the relatively unstable benzo[b] thiophene sulfoxide; its dimerization, followed by dehydrogenation, resulted in the isolation of stable tetracyclic sulfoxides as minor products with cis-dihydrodiols being the dominant metabolites. SMO mainly catalysed the formation of enantioenriched benzo[b] thiophene sulfoxide and 2-methyl benzo[b] thiophene sulfoxides which racemized at ambient temperature. The barriers to pyramidal sulfur inversion of 2- and 3-methyl benzo[b] thiophene sulfoxide metabolites, obtained using TDO and NDO as biocatalysts, were found to be ca.: 25-27 kcal mol(-1). The absolute configurations of the benzo[b] thiophene sulfoxides were determined by ECD spectroscopy, X-ray crystallography and stereochemical correlation. A site-directed mutant E. coli strain containing an engineered form of NDO, was found to change the regioselectivity toward preferential oxidation of the thiophene ring rather than the benzene ring.
PB  - Royal Soc Chemistry, Cambridge
T2  - Organic and Biomolecular Chemistry
T1  - Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes
VL  - 10
IS  - 4
SP  - 782
EP  - 790
DO  - 10.1039/c1ob06678a
ER  - 

@article{
author = "Boyd, Derek R. and Sharma, Narain D. and McMurray, Brian and Haughey, Simon A. and Allen, Christopher C. R. and Hamilton, John T. G. and McRoberts, W. Colin and O'Ferrall, Rory A. More and Nikodinović-Runić, Jasmina and Coulombel, Lydie A. and O'Connor, Kevin E.",
year = "2012",
abstract = "Asymmetric heteroatom oxidation of benzo[b]thiophenes to yield the corresponding sulfoxides was catalysed by toluene dioxygenase (TDO), naphthalene dioxygenase (NDO) and styrene monooxygenase (SMO) enzymes present in P. putida mutant and E. coli recombinant whole cells. TDO-catalysed oxidation yielded the relatively unstable benzo[b] thiophene sulfoxide; its dimerization, followed by dehydrogenation, resulted in the isolation of stable tetracyclic sulfoxides as minor products with cis-dihydrodiols being the dominant metabolites. SMO mainly catalysed the formation of enantioenriched benzo[b] thiophene sulfoxide and 2-methyl benzo[b] thiophene sulfoxides which racemized at ambient temperature. The barriers to pyramidal sulfur inversion of 2- and 3-methyl benzo[b] thiophene sulfoxide metabolites, obtained using TDO and NDO as biocatalysts, were found to be ca.: 25-27 kcal mol(-1). The absolute configurations of the benzo[b] thiophene sulfoxides were determined by ECD spectroscopy, X-ray crystallography and stereochemical correlation. A site-directed mutant E. coli strain containing an engineered form of NDO, was found to change the regioselectivity toward preferential oxidation of the thiophene ring rather than the benzene ring.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Organic and Biomolecular Chemistry",
title = "Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes",
volume = "10",
number = "4",
pages = "782-790",
doi = "10.1039/c1ob06678a"
}

Boyd, D. R., Sharma, N. D., McMurray, B., Haughey, S. A., Allen, C. C. R., Hamilton, J. T. G., McRoberts, W. C., O'Ferrall, R. A. M., Nikodinović-Runić, J., Coulombel, L. A.,& O'Connor, K. E.. (2012). Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes. in Organic and Biomolecular Chemistry
Royal Soc Chemistry, Cambridge., 10(4), 782-790.
https://doi.org/10.1039/c1ob06678a

Boyd DR, Sharma ND, McMurray B, Haughey SA, Allen CCR, Hamilton JTG, McRoberts WC, O'Ferrall RAM, Nikodinović-Runić J, Coulombel LA, O'Connor KE. Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes. in Organic and Biomolecular Chemistry. 2012;10(4):782-790.
doi:10.1039/c1ob06678a .

Boyd, Derek R., Sharma, Narain D., McMurray, Brian, Haughey, Simon A., Allen, Christopher C. R., Hamilton, John T. G., McRoberts, W. Colin, O'Ferrall, Rory A. More, Nikodinović-Runić, Jasmina, Coulombel, Lydie A., O'Connor, Kevin E., "Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes" in Organic and Biomolecular Chemistry, 10, no. 4 (2012):782-790,
https://doi.org/10.1039/c1ob06678a . .