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

A. Riedel; T. Heine; A.H. Westphal; C. Conrad; P. Rathsack; W.J.H. van Berkel; D. Tischler

doi:10.1186/s13568-015-0112-9

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

A. Riedel^*, T. Heine, A.H. Westphal, C. Conrad, P. Rathsack, W.J.H. van Berkel, D. Tischler^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

27 Citations (Scopus)

Abstract

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.

Original language	English
Article number	30
Number of pages	11
Journal	AMB Express
Volume	5
DOIs	https://doi.org/10.1186/s13568-015-0112-9
Publication status	Published - 2015

Keywords

recombinant escherichia-coli
pseudomonas-fluorescens st
functional-analysis
crystal-structure
catabolism genes
strain vlb120
putida ca-3
degradation
mechanism
oxide

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@article{24e627b11d48450dbfdc1af2e521f6f4,

title = "Catalytic and hydrodynamic properties of styrene monooxygenases from Rhocodoccus opacus 1CP are modulated by cofactor binding.",

abstract = "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.",

keywords = "recombinant escherichia-coli, pseudomonas-fluorescens st, functional-analysis, crystal-structure, catabolism genes, strain vlb120, putida ca-3, degradation, mechanism, oxide",

author = "A. Riedel and T. Heine and A.H. Westphal and C. Conrad and P. Rathsack and {van Berkel}, W.J.H. and D. Tischler",

year = "2015",

doi = "10.1186/s13568-015-0112-9",

language = "English",

volume = "5",

journal = "AMB Express",

issn = "2191-0855",

publisher = "Springer",

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TY - JOUR

T1 - Catalytic and hydrodynamic properties of styrene monooxygenases from Rhocodoccus opacus 1CP are modulated by cofactor binding.

AU - Riedel, A.

AU - Heine, T.

AU - Westphal, A.H.

AU - Conrad, C.

AU - Rathsack, P.

AU - van Berkel, W.J.H.

AU - Tischler, D.

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - recombinant escherichia-coli

KW - pseudomonas-fluorescens st

KW - functional-analysis

KW - crystal-structure

KW - catabolism genes

KW - strain vlb120

KW - putida ca-3

KW - degradation

KW - mechanism

KW - oxide

U2 - 10.1186/s13568-015-0112-9

DO - 10.1186/s13568-015-0112-9

M3 - Article

SN - 2191-0855

VL - 5

JO - AMB Express

JF - AMB Express

M1 - 30

ER -

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

Abstract

Keywords

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