English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Chemo‐ and Regioselective Dihydroxylation of Benzene to Hydroquinone Enabled by Engineered Cytochrome P450 Monooxygenase

Zhou, H., Wang, B., Wang, F., Yu, X., Ma, L., Li, A., et al. (2019). Chemo‐ and Regioselective Dihydroxylation of Benzene to Hydroquinone Enabled by Engineered Cytochrome P450 Monooxygenase. Angewandte Chemie International Edition, 58(3), 764-768. doi:10.1002/anie.201812093.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Zhou, Hangyu1, Author
Wang, Binju2, Author
Wang, Fei1, Author
Yu, Xiaojuan1, Author
Ma, Lixin1, Author
Li, Aitao1, Author
Reetz, Manfred T.3, 4, 5, Author           
Affiliations:
1State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan, 430062 P. R. China, ou_persistent22              
2State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 360015 P. R. China, ou_persistent22              
3Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308 China, ou_persistent22              
4Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445588              
5Department of Chemistry, Philipps-University, 35032 Marburg, Germany, ou_persistent22              

Content

show
hide
Free keywords: benzene dihydroxylation; cascade reaction; directed evolution; hydroquinone; P450 monooxygenase
 Abstract: Hydroquinone (HQ) is produced commercially from benzene by multi‐step Hock‐type processes with equivalent amounts of acetone as side‐product. We describe an efficient biocatalytic alternative using the cytochrome P450‐BM3 monooxygenase. Since the wildtype enzyme does not accept benzene, a semi‐rational protein engineering strategy was developed. Highly active mutants were obtained which transform benzene in a one‐pot sequence first into phenol and then regioselectively into HQ without any overoxidation. A computational study shows that the chemoselective oxidation of phenol by the P450‐BM3 variant A82F/A328F leads to the regioselective formation of an epoxide intermediate at the C3=C4 double bond, which departs from the binding pocket and then undergoes fragmentation in aqueous medium with exclusive formation of HQ. As a practical application, an E. coli designer cell system was constructed, which enables the cascade transformation of benzene into the natural product arbutin, which has anti‐inflammatory and anti‐bacterial activities.

Details

show
hide
Language(s): eng - English
 Dates: 2018-10-242018-12-042019-01-14
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201812093
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Angewandte Chemie International Edition
  Other : Angewandte Chemie, International Edition
  Other : Angew. Chem. Int. Ed.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 58 (3) Sequence Number: - Start / End Page: 764 - 768 Identifier: ISSN: 1433-7851
CoNE: https://pure.mpg.de/cone/journals/resource/1433-7851