Aliphatic C[sbnd]H azidation by Mn based mimics of α-ketoglutarate dependent enzymes

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Aliphatic C[sbnd]H azidation by Mn based mimics of α-ketoglutarate dependent enzymes. / Ottenbacher, Roman V.; Lubov, Dmitry P.; Samsonenko, Denis G. et al.

In: Journal of Catalysis, Vol. 429, 115275, 01.2024.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{b8d48eb6182743759c7ecbbe46bcc279,

title = "Aliphatic C[sbnd]H azidation by Mn based mimics of α-ketoglutarate dependent enzymes",

abstract = "α-Ketoglutarate dependent nonheme halogenases catalyze regioselective functionalization of aliphatic C[sbnd]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.",

keywords = "Asymmetric catalysis, Azidation, C-H activation, Enzyme models, Hydrogen peroxide, Manganese",

author = "Ottenbacher, {Roman V.} and Lubov, {Dmitry P.} and Samsonenko, {Denis G.} and Nefedov, {Andrey A.} and Bryliakov, {Konstantin P.}",

note = "This work was supported by the Russian Science Foundation, grant 20-13-00032. AAN is grateful to the Ministry of Science and Higher Education of the Russian Federation, project for Vorozhtsov Novosibirsk Institute of Organic Chemistry (HR-MS measurements), DGS is grateful to the Ministry of Science and Higher Education of the Russian Federation, project for Nikolaev Institute of Inorganic Chemistry (X-ray measurements). The authors thank Dr. M. V. Shashkov and the shared research center “National center of investigation of catalysts” (Boreskov Institute of Catalysis) for the GC-MS measurements.",

year = "2024",

month = jan,

doi = "10.1016/j.jcat.2023.115275",

language = "English",

volume = "429",

journal = "Journal of Catalysis",

issn = "0021-9517",

publisher = "Academic Press Inc.",

}

RIS

TY - JOUR

T1 - Aliphatic C[sbnd]H azidation by Mn based mimics of α-ketoglutarate dependent enzymes

AU - Ottenbacher, Roman V.

AU - Lubov, Dmitry P.

AU - Samsonenko, Denis G.

AU - Nefedov, Andrey A.

AU - Bryliakov, Konstantin P.

N1 - This work was supported by the Russian Science Foundation, grant 20-13-00032. AAN is grateful to the Ministry of Science and Higher Education of the Russian Federation, project for Vorozhtsov Novosibirsk Institute of Organic Chemistry (HR-MS measurements), DGS is grateful to the Ministry of Science and Higher Education of the Russian Federation, project for Nikolaev Institute of Inorganic Chemistry (X-ray measurements). The authors thank Dr. M. V. Shashkov and the shared research center “National center of investigation of catalysts” (Boreskov Institute of Catalysis) for the GC-MS measurements.

PY - 2024/1

Y1 - 2024/1

N2 - α-Ketoglutarate dependent nonheme halogenases catalyze regioselective functionalization of aliphatic C[sbnd]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.

AB - α-Ketoglutarate dependent nonheme halogenases catalyze regioselective functionalization of aliphatic C[sbnd]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.

KW - Asymmetric catalysis

KW - Azidation

KW - C-H activation

KW - Enzyme models

KW - Hydrogen peroxide

KW - Manganese

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85181140936&origin=inward&txGid=2d4ee2873d62bddd867ce79d460a29e0

UR - https://www.mendeley.com/catalogue/999842f9-700e-33b1-a79a-389aacf3036b/

U2 - 10.1016/j.jcat.2023.115275

DO - 10.1016/j.jcat.2023.115275

M3 - Article

VL - 429

JO - Journal of Catalysis

JF - Journal of Catalysis

SN - 0021-9517

M1 - 115275

ER -

ID: 60405853