Excitation Localization/Delocalization Isomerism in a Strongly Coupled Covalent Dimer of 1,3-Diphenylisobenzofuran

2016 ◽  
Vol 120 (20) ◽  
pp. 3473-3483 ◽  
Author(s):  
Joel N. Schrauben ◽  
Akin Akdag ◽  
Jin Wen ◽  
Zdenek Havlas ◽  
Joseph L. Ryerson ◽  
...  
Keyword(s):  
Strongly Coupled ◽  
Covalent Dimer ◽  
Excitation Localization

Strongly coupled nonneutral plasmas : Equilibrium and relaxation in two-component plasmas in Penning-Malmberg trap

2000 ◽  
Vol 10 (PR5) ◽  
pp. Pr5-271-Pr5-274
Author(s):  
H. Totsuji ◽  
K. Tsuruta ◽  
C. Totsuji ◽  
K. Nakano ◽  
T. Kishimoto ◽  
...  
Keyword(s):  
Strongly Coupled ◽  
Nonneutral Plasmas ◽  
Two Component

Nonequilibrium effects in electron-ion strongly coupled plasmas. Molecular dynamics simulation

2000 ◽  
Vol 10 (PR5) ◽  
pp. Pr5-255-Pr5-258 ◽  
Author(s):  
G. E. Norman ◽  
A. A. Valuev ◽  
I. A. Valuev
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Dynamics Simulation ◽  
Strongly Coupled ◽  
Strongly Coupled Plasmas ◽  
Nonequilibrium Effects ◽  
Coupled Plasmas

Loss of dynamic memory in strongly coupled plasmas. Analytic evaluation of the time interval

2000 ◽  
Vol 10 (PR5) ◽  
pp. Pr5-157-Pr5-160
Author(s):  
A. S. Kaklyugin ◽  
G. E. Norman
Keyword(s):  
Time Interval ◽  
Strongly Coupled ◽  
Dynamic Memory ◽  
Strongly Coupled Plasmas ◽  
Analytic Evaluation ◽  
Coupled Plasmas

FAST-ION STOPPING POWER IN HOT, DENSE, STRONGLY-COUPLED PLASMA

1988 ◽  
Vol 49 (C7) ◽  
pp. C7-105-C7-122
Author(s):  
B. J.B. CROWLEY
Keyword(s):  
Stopping Power ◽  
Strongly Coupled ◽  
Strongly Coupled Plasma ◽  
Fast Ion

Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

2019 ◽  
Author(s):  
Christopher John ◽  
Greg M. Swain ◽  
Robert P. Hausinger ◽  
Denis A. Proshlyakov
Keyword(s):  
Active Site ◽  
Structural Model ◽  
Heme Iron ◽  
Chemical Transformations ◽  
Experimental Conditions ◽  
Strongly Coupled ◽  
Non Heme Iron ◽  
Reversible Redox ◽  
Wide Range ◽  
Complex Structural

2-Oxoglutarate (2OG)-dependent dioxygenases catalyze C-H activation while performing a wide range of chemical transformations. In contrast to their heme analogues, non-heme iron centers afford greater structural flexibility with important implications for their diverse catalytic mechanisms. We characterize an <i>in situ</i> structural model of the putative transient ferric intermediate of 2OG:taurine dioxygenase (TauD) by using a combination of spectroelectrochemical and semi-empirical computational methods, demonstrating that the Fe (III/II) transition involves a substantial, fully reversible, redox-linked conformational change at the active site. This rearrangement alters the apparent redox potential of the active site between -127 mV for reduction of the ferric state and 171 mV for oxidation of the ferrous state of the 2OG-Fe-TauD complex. Structural perturbations exhibit limited sensitivity to mediator concentrations and potential pulse duration. Similar changes were observed in the Fe-TauD and taurine-2OG-Fe-TauD complexes, thus attributing the reorganization to the protein moiety rather than the cosubstrates. Redox difference infrared spectra indicate a reorganization of the protein backbone in addition to the involvement of carboxylate and histidine ligands. Quantitative modeling of the transient redox response using two alternative reaction schemes across a variety of experimental conditions strongly supports the proposal for intrinsic protein reorganization as the origin of the experimental observations.

Simulation of two-dimensional cross-relaxation spectra in strongly coupled spin systems

1986 ◽  
Vol 68 (3) ◽  
pp. 515-525 ◽  
Author(s):  
Lewis E Kay ◽  
J.N Scarsdale ◽  
D.R Hare ◽  
J.H Prestegard
Keyword(s):  
Spin Systems ◽  
Cross Relaxation ◽  
Two Dimensional ◽  
Relaxation Spectra ◽  
Strongly Coupled ◽  
Coupled Spin Systems
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