Pressure effects on the radical–radical recombination reaction of photochromic bridged imidazole dimers

2014 ◽  
Vol 16 (33) ◽  
pp. 17537-17540 ◽  
Author(s):  
Katsuya Mutoh ◽  
Jiro Abe

We revealed the structure–entropy relationship of the photochromism of bridged imidazole dimers and that the radical–radical interaction could be controlled by applying high pressure.

1984 ◽  
Vol 142 (1) ◽  
pp. 1-12 ◽  
Author(s):  
H. Hippler ◽  
K. Luther ◽  
A. R. Ravishankara ◽  
J. Troe

1977 ◽  
Vol 66 (2) ◽  
pp. 875-876 ◽  
Author(s):  
M. Lamotte ◽  
S. Risemberg ◽  
A. M. Merle ◽  
J. Joussot‐Dubien

2005 ◽  
Vol 66 (10) ◽  
pp. 1621-1627 ◽  
Author(s):  
P. Thangadurai ◽  
A. Chandra Bose ◽  
S. Ramasamy ◽  
R. Kesavamoorthy ◽  
T.R. Ravindran

ACS Omega ◽  
2021 ◽  
Author(s):  
Ryo Matsumoto ◽  
Sayaka Yamamoto ◽  
Yoshihiko Takano ◽  
Hiromi Tanaka

1975 ◽  
Vol 11 (7) ◽  
pp. 2705-2706 ◽  
Author(s):  
C. Boekema ◽  
F. van der Woude ◽  
G. A. Sawatzky

2014 ◽  
Vol 73 ◽  
pp. 138-143 ◽  
Author(s):  
Yuchuan Tao ◽  
Zbigniew A. Dreger ◽  
Yogendra M. Gupta

1991 ◽  
Vol 69 (11) ◽  
pp. 1699-1704 ◽  
Author(s):  
P. T. T. Wong

Hydrogen/deuterium (H/D) exchange rate constants in chymotrypsinogen have been determined at several pressures up to 28.9 kbar by FTIR spectroscopy. The secondary structure of the protein molecules was monitored simultaneously at the corresponding pressures by the intensity redistribution of the infrared amide I band at these pressures. As in other proteins, the labile protons on the amide groups in chymotrypsinogen can, to a good approximation, be separated into two classes, each with distinct first order H/D exchange rates constants in the time period from 10 min to ~24 h. The fast exchange rate constant increases while the slow exchange rate constant decreases with increasing pressure. The increase in the fast exchange rate constant at high pressure is largely associated with the pressure-induced unfolding of the protein molecules. At extremely high pressure (12.8 kbar), in addition to the unfolding of protein molecules, pressure induced a distortion and weakening of the hydrogen bonds of the fold protein segments also contribute to an increase in the overall H/D exchange rate. The present results confirm that when chymotrypsinogen is dissolved in D2O, a considerable amount of D2O molecules is bound to the protein molecules on the surface as well as in the interior cavities of the molecules. The H/D exchange takes place between these bound D2O and the protons in the protein molecules. The mechanism of the H/D exchange and the interior dynamics in proteins are discussed on the basis of the present results. Key words: hydrogen/deuterium exchange, exchange kinetics, rate constant, pressure effects, infrared spectroscopy, protein, conformation structure, bound water.


Author(s):  
Kenneth E. Prehoda ◽  
Ed S. Mooberry ◽  
John L. Markley

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