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Riedel A, Heine T, Westphal AH, et al. Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding. AMB Express. 2015;5(1):112doi: 10.1186/s13568-015-0112-9.
Riedel, A., Heine, T., Westphal, A. H., Conrad, C., Rathsack, P., van Berkel, W. J., & Tischler, D. (2015). Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding. AMB Express, 5(1), 112. https://doi.org/10.1186/s13568-015-0112-9
Riedel, Anika, et al. "Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding." AMB Express vol. 5,1 (2015): 112. doi: https://doi.org/10.1186/s13568-015-0112-9
Riedel A, Heine T, Westphal AH, Conrad C, Rathsack P, van Berkel WJ, Tischler D. Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding. AMB Express. 2015 Dec;5(1):112. doi: 10.1186/s13568-015-0112-9. Epub 2015 Jun 04. PMID: 26054733; PMCID: PMC4460183.
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AMB Express. 2015 Dec;5(1):112. doi: 10.1186/s13568-015-0112-9. Epub 2015 Jun 04.

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

AMB Express

Anika Riedel, Thomas Heine, Adrie H Westphal, Catleen Conrad, Philipp Rathsack, Willem J H van Berkel, Dirk Tischler

Affiliations

  1. Interdisciplinary Ecological Center, Freiberg Environmental Microbiology Group, TU Bergakademie Freiberg, Leipziger Str. 29, 09599, Freiberg, Germany, [email protected].

PMID: 26054733 PMCID: PMC4460183 DOI: 10.1186/s13568-015-0112-9

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.

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