Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding

Styrene monooxygenases (SMOs) are flavoenzymes catalyzing the epoxidation of styrene into styrene oxide. SMOs are composed of a monooxygenase (StyA) and a reductase (StyB). The latter delivers reduced FAD to StyA on the expense of NADH. We identified Rhodococcus opacus 1CP as the first microorganism...

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Autores principales: Riedel, Anika, Heine, Thomas, Westphal, Adrie H, Conrad, Catleen, Rathsack, Philipp, van Berkel, Willem J H, Tischler, Dirk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2015
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4460183/
https://www.ncbi.nlm.nih.gov/pubmed/26054733
http://dx.doi.org/10.1186/s13568-015-0112-9
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author Riedel, Anika
Heine, Thomas
Westphal, Adrie H
Conrad, Catleen
Rathsack, Philipp
van Berkel, Willem J H
Tischler, Dirk
author_facet Riedel, Anika
Heine, Thomas
Westphal, Adrie H
Conrad, Catleen
Rathsack, Philipp
van Berkel, Willem J H
Tischler, Dirk
author_sort Riedel, Anika
collection PubMed
description Styrene monooxygenases (SMOs) are flavoenzymes catalyzing the epoxidation of styrene into styrene oxide. SMOs are composed of a monooxygenase (StyA) and a reductase (StyB). The latter delivers reduced FAD to StyA on the expense of NADH. We identified Rhodococcus opacus 1CP as the first microorganism to possess three different StyA isoforms occurring in two systems StyA1/StyA2B and StyA/StyB, respectively. The hydrodynamic properties of StyA isozymes were found to be modulated by the binding of the (reduced) FAD cofactor. StyA1 and SyA2B mainly occur as dimers in their active forms while StyA is a monomer. StyA1 showed the highest epoxidation activity and excellent enantioselectivity in aromatic sulfoxidation. The hydrodynamic and biocatalytic properties of SMOs from strain 1CP are of relevance for investigation of possible industrial applications. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13568-015-0112-9) contains supplementary material, which is available to authorized users.
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spelling pubmed-44601832015-06-15 Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding Riedel, Anika Heine, Thomas Westphal, Adrie H Conrad, Catleen Rathsack, Philipp van Berkel, Willem J H Tischler, Dirk AMB Express Original Article Styrene monooxygenases (SMOs) are flavoenzymes catalyzing the epoxidation of styrene into styrene oxide. SMOs are composed of a monooxygenase (StyA) and a reductase (StyB). The latter delivers reduced FAD to StyA on the expense of NADH. We identified Rhodococcus opacus 1CP as the first microorganism to possess three different StyA isoforms occurring in two systems StyA1/StyA2B and StyA/StyB, respectively. The hydrodynamic properties of StyA isozymes were found to be modulated by the binding of the (reduced) FAD cofactor. StyA1 and SyA2B mainly occur as dimers in their active forms while StyA is a monomer. StyA1 showed the highest epoxidation activity and excellent enantioselectivity in aromatic sulfoxidation. The hydrodynamic and biocatalytic properties of SMOs from strain 1CP are of relevance for investigation of possible industrial applications. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13568-015-0112-9) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2015-06-04 /pmc/articles/PMC4460183/ /pubmed/26054733 http://dx.doi.org/10.1186/s13568-015-0112-9 Text en © Riedel et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Riedel, Anika
Heine, Thomas
Westphal, Adrie H
Conrad, Catleen
Rathsack, Philipp
van Berkel, Willem J H
Tischler, Dirk
Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
title Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
title_full Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
title_fullStr Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
title_full_unstemmed Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
title_short Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding
title_sort catalytic and hydrodynamic properties of styrene monooxygenases from rhodococcus opacus 1cp are modulated by cofactor binding
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4460183/
https://www.ncbi.nlm.nih.gov/pubmed/26054733
http://dx.doi.org/10.1186/s13568-015-0112-9
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