512787-29-0Relevant articles and documents
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.
An efficient method for one-carbon elongation of aryl aldehydes via their dibromoalkene derivatives
Huh, Dal Ho,Jeong, Ji Sang,Lee, Hee Bong,Ryu, Hoejin,Kim, Young Gyu
, p. 9925 - 9932 (2007/10/03)
Various aryl aldehydes were efficiently converted into one-carbon extended aryl acetamides or aryl acetic acids through the reaction of their dibromoalkene derivatives with pyrrolidine in the presence of water under very mild conditions.
