Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1103/PhysRevLett.67.679 | DOI Listing |
J Chem Phys
October 2023
School of Chemical and Biomolecular Sciences, Southern Illinois University Carbondale, 1245 Lincoln Drive MC 4409, Carbondale, Illinois 62901, USA.
Enzymes accelerate the rates of biomolecular reactions by many orders of magnitude compared to bulk solution, and it is widely understood that this catalytic effect arises from a combination of polar pre-organization and electrostatic transition state stabilization. A number of recent reports have also implicated ultrafast (femtosecond-picosecond) timescale motions in enzymatic activity. However, complications arising from spatially-distributed disorder, the occurrence of multiple substrate binding modes, and the influence of hydration dynamics on solvent-exposed active sites still confound many experimental studies.
View Article and Find Full Text PDFJ Chem Phys
December 2004
Department of Chemistry, Graduate School of Science, Tohoku University, Sendai, 980-8578, Japan.
A picosecond time-resolved IR-UV pump-probe spectroscopic study was carried out for the intramolecular vibrational energy redistribution of the OH/OD stretching vibration of isolated phenol and its isotopomers in supersonic beams. The time evolution due to IVR showed a significant isotope effect; the OH stretch vibration showed a single exponential decay and its lifetime is greatly lengthened upon the deuterium substitution of the CH group. The OD stretch vibration exhibited prominent quantum beats.
View Article and Find Full Text PDFPhys Rev B Condens Matter
January 1995
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!