Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: Engineering Fe(II)/α-ketoglutarate-dependent halogenases and desaturases
Authors: Papadopoulou, Athena
Meyer, Fabian
Buller, Rebecca M.
et. al: No
DOI: 10.1021/acs.biochem.2c00115
Published in: Biochemistry
Issue Date: 21-Apr-2022
Publisher / Ed. Institution: American Chemical Society
ISSN: 0006-2960
1520-4995
Language: English
Subjects: Hydrogen abstraction; Organic reaction; Halogenation; Monomer
Subject (DDC): 572: Biochemistry
Abstract: Fe(II)/α-ketoglutarate-dependent dioxygenases (α-KGDs) are widespread enzymes in aerobic biology and serve a remarkable array of biological functions, including roles in collagen biosynthesis, plant and animal development, transcriptional regulation, nucleic acid modification, and secondary metabolite biosynthesis. This functional diversity is reflected in the enzymes' catalytic flexibility as α-KGDs can catalyze an intriguing set of synthetically valuable reactions, such as hydroxylations, halogenations, and desaturations, capturing the interest of scientists across disciplines. Mechanistically, all α-KGDs are understood to follow a similar activation pathway to generate a substrate radical, yet how individual members of the enzyme family direct this key intermediate toward the different reaction outcomes remains elusive, triggering structural, computational, spectroscopic, kinetic, and enzyme engineering studies. In this Perspective, we will highlight how first enzyme and substrate engineering examples suggest that the chemical reaction pathway within α-KGDs can be intentionally tailored using rational design principles. We will delineate the structural and mechanistic investigations of the reprogrammed enzymes and how they begin to inform about the enzymes' structure-function relationships that determine chemoselectivity. Application of this knowledge in future enzyme and substrate engineering campaigns will lead to the development of powerful C-H activation catalysts for chemical synthesis.
URI: https://digitalcollection.zhaw.ch/handle/11475/25299
Fulltext version: Published version
License (according to publishing contract): Licence according to publishing contract
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:Publikationen Life Sciences und Facility Management

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