Dual-function enzyme catalysis for enantioselective carbon–nitrogen bond formation

Introduction: Aza-Michael addition is an important reaction for carbon-nitrogen bond formation in synthetic organic chemistry. Expalantion: Conjugate addition of imidazole to α,β-unsaturated carbonyl/cyano compounds provides significant numbers of the biologically and synthetically interesting products, such as β-amino acids and β-lactams, which have attracted great attention for their use as key intermediates of anticancer agents, antibiotics and other drugs. Conclusion: This review addresses most significant method for the synthesis of N-substituted imidazole derivatives following Michael addition reaction of imidazole to α,β-unsaturated carbonyl/cyano compounds using ionic liquid/base/acid/enzyme as catalysts from year 2007-2017.

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Correction to Nitrogen–Nitrogen Bond Formation via a Substrate-Bound Anion at a Mononuclear Nickel Platform

Organometallics ◽

10.1021/acs.organomet.8b00126 ◽

2018 ◽

Vol 37 (6) ◽

pp. 1086-1086 ◽

Cited By ~ 1

Author(s):

Mikhail D. Kosobokov ◽

Aaron Sandleben ◽

Nicolas Vogt ◽

Axel Klein ◽

David A. Vicic

Keyword(s):

Bond Formation ◽

Nitrogen Bond

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Light-driven carbon−carbon bond formation via CO2reduction catalyzed by complexes of CdS nanorods and a 2-oxoacid oxidoreductase

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1903948116 ◽

2019 ◽

Vol 117 (1) ◽

pp. 135-140 ◽

Cited By ~ 5

Author(s):

Hayden Hamby ◽

Bin Li ◽

Katherine E. Shinopoulos ◽

Helena R. Keller ◽

Sean J. Elliott ◽

...

Keyword(s):

Conformational Changes ◽

Enzyme Catalysis ◽

Transient Absorption ◽

Tricarboxylic Acid Cycle ◽

Semiconductor Nanocrystals ◽

Bond Formation ◽

Critical Role ◽

Transient Absorption Spectroscopy ◽

Carbon Bond ◽

Carbon Carbon Bond

Redox enzymes are capable of catalyzing a vast array of useful reactions, but they require redox partners that donate or accept electrons. Semiconductor nanocrystals provide a mechanism to convert absorbed photon energy into redox equivalents for enzyme catalysis. Here, we describe a system for photochemical carbon−carbon bond formation to make 2-oxoglutarate by coupling CO2with a succinyl group. Photoexcited electrons from cadmium sulfide nanorods (CdS NRs) transfer to 2-oxoglutarate:ferredoxin oxidoreductase fromMagnetococcus marinusMC-1 (MmOGOR), which catalyzes a carbon−carbon bond formation reaction. We thereby decouple MmOGOR from its native role in the reductive tricarboxylic acid cycle and drive it directly with light. We examine the dependence of 2-oxoglutarate formation on a variety of factors and, using ultrafast transient absorption spectroscopy, elucidate the critical role of electron transfer (ET) from CdS NRs to MmOGOR. We find that the efficiency of this ET depends strongly on whether the succinyl CoA (SCoA) cosubstrate is bound at the MmOGOR active site. We hypothesize that the conformational changes due to SCoA binding impact the CdS NR−MmOGOR interaction in a manner that decreases ET efficiency compared to the enzyme with no cosubstrate bound. Our work reveals structural considerations for the nano−bio interfaces involved in light-driven enzyme catalysis and points to the competing factors of enzyme catalysis and ET efficiency that may arise when complex enzyme reactions are driven by artificial light absorbers.

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