Efficient biocatalytic C–H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450-Reference-Cited by-同舟云学术

Efficient biocatalytic C–H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450

Published:2023 Issue:90 Volume:59 Page:13486-13489
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Gee Alecia R.¹^ORCID,Stone Isobella S. J.¹^ORCID,Stockdale Tegan P.²^ORCID,Pukala Tara L.¹^ORCID,De Voss James J.²^ORCID,Bell Stephen G.¹^ORCID

Affiliation:

1. School of Physics, Chemistry and Earth Sciences, University of Adelaide, Adelaide, SA 5005, Australia

2. School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld, 4072, Australia

Abstract

The replacement of specific residues of an archaeal thermostable heme monooxygenase enzyme enabled its conversion to a highly stable peroxygenase allowing the efficient and selective oxidation of unactivated C–H bonds at elevated temperatures.

Funder

Australian Research Council

Australian Government

Commonwealth Scientific and Industrial Research Organisation

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CC/D3CC04626E

Reference25 articles.

1. Unrivalled diversity: the many roles and reactions of bacterial cytochromes P450 in secondary metabolism

2. Enzymatic Late‐Stage Modifications: Better Late Than Never

3. Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications

4. Scalable biocatalytic C–H oxyfunctionalization reactions

5. The taming of oxygen: biocatalytic oxyfunctionalisations

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