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 . .