Aliphatic C-H Azidation by Mn Based Mimics of α-Ketoglutarate Dependent Enzymes | Sciact - CRIS-system of Boreskov Institute of Catalysis

Aliphatic C-H Azidation by Mn Based Mimics of α-Ketoglutarate Dependent Enzymes Full article

Journal

Journal of Catalysis
ISSN: 0021-9517 , E-ISSN: 1090-2694

Output data

Year: 2024, Volume: 429, Article number : 115275, Pages count : 6 DOI: 10.1016/j.jcat.2023.115275

Tags

Asymmetric catalysis; Azidation; C-H activation; Enzyme models; Hydrogen peroxide; Manganese

Authors

Ottenbacher Roman V. ¹ , Lubov Dmitry P. ¹ , Samsonenko Denis G. ^2,3 , Nefedov Andrey A. ^3,4 , Bryliakov Konstantin P. ¹

Affiliations

1	Zelinsky Institute of Organic Chemistry RAS, Leninsky Pr. 47, Moscow 119991, Russia
2	Nikolaev Institute of Inorganic Chemistry SB RAS, Pr. Lavrentieva 3, Novosibirsk 630090, Russia
3	Novosibirsk State University, Pirogova 1, Novosibirsk 630090, Russia
4	Vorozhtsov Novosibirsk Institute of Organic Chemistry SB RAS, Pr. Lavrentieva 9, Novosibirsk 630090, Russia

α-Ketoglutarate dependent nonheme halogenases catalyze regioselective functionalization of aliphatic C-H bonds via H abstraction by the ferryl site of the [X−FeIV=O] intermediate, followed by radical rebound to an adjacent halogen ligand X at the same Fe center. Herein we report biomimetic nonheme Mn complexes, possessing two labile cis-α coordination sites and capable of catalyzing the enantioselective azidation of C(sp3)−H groups. Proper ligand environment of the active sites imposes steric constraints on HO−Mn rebound, thus accounting for preferential C-radical rebound to the adjacent N3−Mn ligand. Such mechanism of selectivity control is analogous to that operating in the prototypical α-ketoglutarate-dependent nonheme iron halogenases.

Ottenbacher R.V. , Lubov D.P. , Samsonenko D.G. , Nefedov A.A. , Bryliakov K.P.
Aliphatic C-H Azidation by Mn Based Mimics of α-Ketoglutarate Dependent Enzymes
Journal of Catalysis. 2024. V.429. 115275 :1-6. DOI: 10.1016/j.jcat.2023.115275 WOS Scopus ANCAN OpenAlex

Submitted:	Nov 21, 2023
Accepted:	Dec 21, 2023
Published online:	Dec 27, 2023
Published print:	Jan 1, 2024

Web of science:	WOS:001166120900001
Scopus:	2-s2.0-85181140936
Chemical Abstracts:	2024:47014
Chemical Abstracts (print):	185:313206
OpenAlex:	W4390277711

DB	Citing
OpenAlex	3
Web of science	3
Scopus	3