A Comparison of the Energetics of Proton Transfer in the Serine and Cysteine “Charge Relay” Systems and the Role of the Protein Electrostatic Potential on the Proton Transfer Energetics

1979 ◽  
pp. 77-90 ◽  
Author(s):  
David M. Hayes ◽  
Peter A. Kollman
Keyword(s):  
Proton Transfer ◽  
Electrostatic Potential ◽  
Transfer Energetics ◽  
Relay Systems

The Role of Conserved Residues in the DEDDh Motif: the Proton-Transfer Mechanism of HIV-1 RNase H

ACS Catalysis ◽  
2021 ◽  
pp. 7915-7927
Author(s):  
Simon L. Dürr ◽  
Olga Bohuszewicz ◽  
Dénes Berta ◽  
Reynier Suardiaz ◽  
Pablo G. Jambrina ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Rnase H ◽  
Transfer Mechanism ◽  
Conserved Residues ◽  
Hiv 1

scholarly journals Revealing the role of excited state proton transfer (ESPT) in excited state hydrogen transfer (ESHT): systematic study in phenol–(NH3)n clusters

2021 ◽  
Author(s):  
Christophe Jouvet ◽  
Mitsuhiko Miyazaki ◽  
Masaaki Fujii
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Systematic Study ◽  
General Model ◽  
Hydrogen Transfer ◽  
Excited State Proton Transfer

A general model of excited state hydrogen transfer (ESHT) which unifies ESHT and the excited state proton transfer (ESPT) is presented from experimental and theoretical works on phenol–(NH3)n. The hidden role of ESPT is revealed.

Role of Solvent in Excited-State Proton Transfer in Hypericin

1994 ◽  
Vol 98 (34) ◽  
pp. 8352-8358 ◽  
Author(s):  
F. Gai ◽  
M. J. Fehr ◽  
J. W. Petrich
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Excited State Proton Transfer ◽  
Role Of Solvent

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

Role of Water in Catalyzing Proton Transfer in Glucose Dehydration to 5-Hydroxymethylfurfural

ChemCatChem ◽  
2017 ◽  
Vol 9 (14) ◽  
pp. 2784-2789 ◽  
Author(s):  
Feng Zhou ◽  
Xiang Sun ◽  
Di Wu ◽  
Yugen Zhang ◽  
Haibin Su
Keyword(s):  
Proton Transfer

Isolated complexes of the amino acid arginine with polyether and polyamine macrocycles, the role of proton transfer

2017 ◽  
Vol 19 (46) ◽  
pp. 31345-31351 ◽  
Author(s):  
Juan Ramón Avilés-Moreno ◽  
Giel Berden ◽  
Jos Oomens ◽  
Bruno Martínez-Haya
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Proton Transfer ◽  
Acid Group ◽  
Side Group ◽  
Carboxylic Acid Group

Protonated arginine interacts with 12-crown-4 through the guanidinium side group. In the complex with the N-substituted analog cyclen, the dominant conformation is the result of the proton transfer from the carboxylic acid group of the amino acid to the macrocycle.

Mechanistic Studies of the Hydroamination of Norbornene with Electrophilic Platinum Complexes: The Role of Proton Transfer

2008 ◽  
Vol 130 (49) ◽  
pp. 16562-16571 ◽  
Author(s):  
Jennifer L. McBee ◽  
Alexis T. Bell ◽  
T. Don Tilley
Keyword(s):  
Proton Transfer ◽  
Platinum Complexes ◽  
Mechanistic Studies

Pathway of Proton Transfer in Bacterial Reaction Centers: Role of Aspartate-L213 in Proton Transfers Associated with Reduction of Quinone to Dihydroquinone

Biochemistry ◽  
1994 ◽  
Vol 33 (3) ◽  
pp. 734-745 ◽  
Author(s):  
M. L. Paddock ◽  
S. H. Rongey ◽  
P. H. McPherson ◽  
A. Juth ◽  
G. Feher ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Reaction Centers ◽  
Bacterial Reaction Centers ◽  
Proton Transfers

1H NMR studies of proton transfer equilibria in hydrogen bonds – the role of the entropy

2001 ◽  
Vol 79 (9) ◽  
pp. 1376-1380 ◽  
Author(s):  
Roland Langner ◽  
Georg Zundel
Keyword(s):  
Hydrogen Bonds ◽  
Proton Transfer ◽  
Nmr Studies ◽  
H Nmr
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