title: Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus 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.
authors.affiliation: Interdisciplinary Ecological Center, Freiberg Environmental Microbiology Group, TU Bergakademie Freiberg, Leipziger Str. 29, 09599, Freiberg, Germany, anika.riedel@ioez.tu-freiberg.de.
authors.forename: Anika
authors.initials: A
authors.lastname: Riedel
authors.forename: Thomas
authors.initials: T
authors.lastname: Heine
authors.forename: Adrie H
authors.initials: AH
authors.lastname: Westphal
authors.forename: Catleen
authors.initials: C
authors.lastname: Conrad
authors.forename: Philipp
authors.initials: P
authors.lastname: Rathsack
authors.forename: Willem J H
authors.initials: WJ
authors.lastname: van Berkel
authors.forename: Dirk
authors.initials: D
authors.lastname: Tischler