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Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Enzymes
1998Acetylcholinesterase (AChE) and chymotrypsin are serine enzymes whose catalytic mechanism involves a nucleophilic attack (serine) and a general acid-base moiety (histidine). The incipient imidiazolium which is formed as a result of the nucleophilic attack by serine is stabilized by the negatively charged carboxylate (Glu or Asp).
Rohit Medhekar +4 more
openaire +1 more source
Visible Light-Driven Radical-Mediated C–C Bond Cleavage/Functionalization in Organic Synthesis
Chemical Reviews, 2021Jia-Rong Chen, Wen-Jing Xiao
exaly
Electrochemical Oxidation Induced Selective C–C Bond Cleavage
Chemical Reviews, 2021Yujie Liang, Ning Jiao
exaly
Journal of the American Chemical Society, 2006
C. Fuhrmann, M. Daugherty, D. Agard
semanticscholar +1 more source
C. Fuhrmann, M. Daugherty, D. Agard
semanticscholar +1 more source
Transition-Metal-Catalyzed C–H Bond Activation for the Formation of C–C Bonds in Complex Molecules
Chemical Reviews, 2023Jamie Docherty, , Michael T Findlay
exaly
A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment.
Science, 1997Elissa L. Ash +3 more
semanticscholar +1 more source
First-Row d-Block Element-Catalyzed Carbon–Boron Bond Formation and Related Processes
Chemical Reviews, 2021Shubhankar Kumar Bose +2 more
exaly

