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

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 : DOI: 10.1016/j.jcat.2023.115275

Authors

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

Affiliations

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

α-Ketoglutarate dependent nonheme halogenases catalyze regioselective functionalization of aliphatic Csingle bondH 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 . DOI: 10.1016/j.jcat.2023.115275 WOS OpenAlex

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