Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 411994
Title Catalytic and structural features of flavoprotein hydroxylases and epoxidases
Author(s) Montersino, S.; Tischler, D.; Gassner, G.T.; Berkel, W.J.H. van
Source Advanced Synthesis and Catalysis 353 (2011)13. - ISSN 1615-4150 - p. 2301 - 2319.
Department(s) Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) p-hydroxybenzoate hydroxylase - 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase - recombinant escherichia-coli - fad-dependent monooxygenase - rhodococcus-opacus 1cp - whole-cell biocatalyst - styrene monooxygenase - phenol hydroxylase - crystal-structure
Abstract Monooxygenases perform chemo-, regio- and/or enantioselective oxygenations of organic substrates under mild reaction conditions. These properties and the increasing number of representatives along with effective preparation methods place monooxygenases in the focus of industrial biocatalysis. Mechanistic and structural insights reveal reaction sequences and allow turning them into efficient tools for the production of valuable products. Herein we describe two biocatalytically relevant subclasses of flavoprotein monooxygenases with a close evolutionary relation: subclass A represented by p-hydroxybenzoate hydroxylase (PHBH) and subclass E formed by styrene monooxygenases (SMOs). PHBH family members perform highly regioselective hydroxylations on a wide variety of aromatic compounds. The more recently discovered SMOs catalyze a number of stereoselective epoxidation and sulfoxidation reactions. Mechanistic and structural studies expose distinct characteristics, which provide a promising source for future biocatalyst development.
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