FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase

D. Tischler; M. Schlömann; W.J.H. van Berkel; G.T. Gassner

doi:10.1016/j.febslet.2013.10.013

FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase

D. Tischler, M. Schlömann, W.J.H. van Berkel, G.T. Gassner

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16 Citations (Scopus)

Abstract

StyA2B represents a new class of styrene monooxygenases that integrates flavin-reductase and styrene-epoxidase activities into a single polypeptide. This naturally-occurring fusion protein offers new avenues for studying and engineering biotechnologically relevant enantioselective biochemical epoxidation reactions. Stopped-flow kinetic studies of StyA2B reported here identify reaction intermediates similar to those reported for the separate reductase and epoxidase components of related two-component systems. Our studies identify substrate epoxidation and elimination of water from the FAD C(4a)-hydroxide as rate-limiting steps in the styrene epoxidation reaction. Efforts directed at accelerating these reaction steps are expected to greatly increase catalytic efficiency and the value of StyA2B as biocatalyst.

Original language	English
Pages (from-to)	3848-3852
Journal	FEBS Letters
Volume	587
Issue number	23
DOIs	https://doi.org/10.1016/j.febslet.2013.10.013
Publication status	Published - 2013

Keywords

rhodococcus-opacus 1cp
phenol hydroxylase
wild-type
mechanism

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title = "FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase",

abstract = "StyA2B represents a new class of styrene monooxygenases that integrates flavin-reductase and styrene-epoxidase activities into a single polypeptide. This naturally-occurring fusion protein offers new avenues for studying and engineering biotechnologically relevant enantioselective biochemical epoxidation reactions. Stopped-flow kinetic studies of StyA2B reported here identify reaction intermediates similar to those reported for the separate reductase and epoxidase components of related two-component systems. Our studies identify substrate epoxidation and elimination of water from the FAD C(4a)-hydroxide as rate-limiting steps in the styrene epoxidation reaction. Efforts directed at accelerating these reaction steps are expected to greatly increase catalytic efficiency and the value of StyA2B as biocatalyst.",

keywords = "rhodococcus-opacus 1cp, phenol hydroxylase, wild-type, mechanism",

author = "D. Tischler and M. Schl{\"o}mann and {van Berkel}, W.J.H. and G.T. Gassner",

year = "2013",

doi = "10.1016/j.febslet.2013.10.013",

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TY - JOUR

T1 - FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase

AU - Tischler, D.

AU - Schlömann, M.

AU - van Berkel, W.J.H.

AU - Gassner, G.T.

PY - 2013

Y1 - 2013

N2 - StyA2B represents a new class of styrene monooxygenases that integrates flavin-reductase and styrene-epoxidase activities into a single polypeptide. This naturally-occurring fusion protein offers new avenues for studying and engineering biotechnologically relevant enantioselective biochemical epoxidation reactions. Stopped-flow kinetic studies of StyA2B reported here identify reaction intermediates similar to those reported for the separate reductase and epoxidase components of related two-component systems. Our studies identify substrate epoxidation and elimination of water from the FAD C(4a)-hydroxide as rate-limiting steps in the styrene epoxidation reaction. Efforts directed at accelerating these reaction steps are expected to greatly increase catalytic efficiency and the value of StyA2B as biocatalyst.

AB - StyA2B represents a new class of styrene monooxygenases that integrates flavin-reductase and styrene-epoxidase activities into a single polypeptide. This naturally-occurring fusion protein offers new avenues for studying and engineering biotechnologically relevant enantioselective biochemical epoxidation reactions. Stopped-flow kinetic studies of StyA2B reported here identify reaction intermediates similar to those reported for the separate reductase and epoxidase components of related two-component systems. Our studies identify substrate epoxidation and elimination of water from the FAD C(4a)-hydroxide as rate-limiting steps in the styrene epoxidation reaction. Efforts directed at accelerating these reaction steps are expected to greatly increase catalytic efficiency and the value of StyA2B as biocatalyst.

KW - rhodococcus-opacus 1cp

KW - phenol hydroxylase

KW - wild-type

KW - mechanism

U2 - 10.1016/j.febslet.2013.10.013

DO - 10.1016/j.febslet.2013.10.013

M3 - Article

SN - 0014-5793

VL - 587

SP - 3848

EP - 3852

JO - FEBS Letters

JF - FEBS Letters

IS - 23

ER -

FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase

Abstract

Keywords

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