151647-54-0Relevant articles and documents
Reductive ipso-radical cyclization onto aromatic rings of five-membered alicyclic amino acids bearing N-(2-phenyl)benzoyl groups by photoinduced electron transfer promoted decarboxylation
Yamada, Tomoaki,Ozaki, Yui,Yamawaki, Mugen,Sugiura, Yoshihiko,Nishino, Kana,Morita, Toshio,Yoshimi, Yasuharu
, p. 835 - 838 (2017)
A new radical cyclization has been developed for the one-step synthesis of spiro dihydroisoquinolinone derivatives from alicyclic amino acids bearing N-(2-phenyl)benzoyl groups through photoinduced electron transfer (PET)-promoted decarboxylation. Reductive ipso-radical cyclization onto a benzene ring by an alkyl radical is achieved under mild conditions for the first time, although the substrates are limited to five-membered aliphatic carboxylic acids bearing N-(2-phenyl)benzoyl groups.
Efficiency Enhancement of a Photocatalytic Decarbonylation of an Aminocyclopropenone by Benzothiophene Substitution
Mishiro, Kenji,Nomura, Mitsuki,Furuyama, Taniyuki,Kunishima, Munetaka
, p. 3625 - 3636 (2021/03/03)
To improve the efficiency of the photocatalytic decarbonylation of cyclopropenones, the effects of substituents on cyclopropenone were explored. A benzothiophene-substituted aminocyclopropenone exhibited significantly improved decarbonylation efficiency t
Photoenzymatic Reductions Enabled by Direct Excitation of Flavin-Dependent "Ene"-Reductases
Sandoval, Braddock A.,Clayman, Phillip D.,Oblinsky, Daniel G.,Oh, Seokjoon,Nakano, Yuji,Bird, Matthew,Scholes, Gregory D.,Hyster, Todd K.
supporting information, p. 1735 - 1739 (2021/01/25)
Non-natural photoenzymatic reactions reported to date have depended on the excitation of electron donor-acceptor complexes formed between substrates and cofactors within protein active sites to facilitate electron transfer. While this mechanism has unlocked new reactivity, it limits the types of substrates that can be involved in this area of catalysis. Here we demonstrate that direct excitation of flavin hydroquinone within "ene"-reductase active sites enables new substrates to participate in photoenzymatic reactions. We found that by using photoexcitation these enzymes gain the ability to reduce acrylamides through a single electron transfer mechanism.