Structure-activity relationship studies in single-site esterase peptide dendrimers
We recently reported on peptide dendrimers with a single catalytic site at the dendrimer core catalyzing the hydrolysis of acetoxy- and butyryloxy-pyrene trisulfonate 1a/b in aqueous buffer with Michaelis-Menten kinetics. Substrate binding is mediated by
Excited-State Proton-Transfer Kinetics: A Theoretical Model
The intersecting-state model is applied to excited state proton-transfer reactions.The results are consistent with those previously obtained for the analogous ground-state reactions.The transition-state bond order n* is similar in the ground and excited states: carbon acids have lower n* than nitrogen or oxygen acids.The mixing entropy parameter λ is found to be lower for excited-state than ground-state reactions.The mechanistic implications of this are discussed.
Arnaut, Luis G.,Formosinho, Sebastiao J.
p. 685 - 691
(2007/10/02)
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