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  P450-BM3-Catalyzed Sulfoxidation versus Hydroxylation: A Common or Two Different Catalytically Active Species?

Wang, J.-b., Huang, Q., Peng, W., Wu, P., Yu, D., Chen, B., et al. (2020). P450-BM3-Catalyzed Sulfoxidation versus Hydroxylation: A Common or Two Different Catalytically Active Species? Journal of the American Chemical Society, 142(4), 2068-2073. doi:10.1021/jacs.9b13061.

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 Creators:
Wang, Jian-bo1, Author
Huang, Qun1, Author
Peng, Wei2, Author
Wu, Peng2, Author
Yu, Da1, Author
Chen, Bo1, Author
Wang, Binju2, Author
Reetz, Manfred T.3, 4, Author           
Affiliations:
1Key Laboratory of Phytochemistry R&D of Hunan Province, College of Chemistry and Chemical Engineering, Key Laboratory of Chemical Biology and Traditional Chinese Medicine Research (Ministry of Education), College of Chemistry and Chemical Engineering, Hunan Normal University, 410081 Changsha, People’s Republic of 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              
3Chemistry Department, Philipps-University, Hans-Meerwein-Strasse 4, 35032 Marburg, Germany, ou_persistent22              
4Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445588              

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 Abstract: While the mechanism of the P450-catalyzed oxidative hydroxylation of organic compounds has been studied in detail for many years, less is known about sulfoxidation. Depending upon the structure of the respective substrate, heme-Fe═O (Cpd I), heme–Fe(III)–OOH (Cpd 0), and heme–Fe(III)–H2O2 (protonated Cpd 0) have been proposed as reactive intermediates. In the present study, we consider the transformation of isosteric substrates via sulfoxidation and oxidative hydroxylation, respectively, catalyzed by regio- and enantioselective mutants of P450-BM3 which were constructed by directed evolution. 1-Thiochromanone and 1-tetralone were used as the isosteric substrates because, unlike previous studies involving fully flexible compounds such as thia-fatty acids and fatty acids, respectively, these compounds are rigid and cannot occur in a multitude of different conformations and binding modes in the large P450-BM3 binding pocket. The experimental results comprising activity and regio- and enantioselectivity, flanked by molecular dynamics computations within a time scale of 300 ns and QM/MM calculations of transition-state energies, unequivocally show that heme-Fe═O (Cpd I) is the common catalytically active intermediate in both sulfoxidation and oxidative hydroxylation.

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Language(s): eng - English
 Dates: 2019-12-042020-01-132020-01-29
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.9b13061
 Degree: -

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Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 142 (4) Sequence Number: - Start / End Page: 2068 - 2073 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870