scholarly journals Assesment of the Proton Donor Capacity as a Marker of Anti-Oxidative Defense in Premature New Borns

2011 ◽  
Vol 70 ◽  
pp. 678-678
Author(s):  
M Matyas ◽  
G Zaharie ◽  
M Popa ◽  
L Blaga ◽  
S Andreica ◽  
...  



1976 ◽  
Vol 7 (13) ◽  
pp. no-no
Author(s):  
N. S. PIVNENKO ◽  
O. V. LAVRUSHINA ◽  
L. M. GRIN ◽  
V. F. LAVRUSHIN


Author(s):  
L. E. Vinogradova ◽  
L. A. Leites ◽  
A. I. Kovredov ◽  
V. A. Ol'shevskaya ◽  
L. I. Zakharkin


1984 ◽  
Vol 20 (1) ◽  
pp. 29-33 ◽  
Author(s):  
T. B. Vishnyakova ◽  
V. K. Pogorelyi




2018 ◽  
Author(s):  
Sandepan Maity ◽  
Robert Flowers

Despite the broad utility and application of SmI<sub>2</sub>in synthesis, the reagent is used in stoichiometric amounts and has a high molecular weight, resulting in a large amount of material being used for reactions requiring one or more equivalents of electrons. We report mechanistic studies on catalytic reactions of Sm(II) employing a terminal magnesium reductant and trimethyl silyl chloride in concert with a non-coordinating proton donor source. Reactions using this approach permitted reductions with as little as 1 mol% Sm. The mechanistic approach enabled catalysis employing HMPA as a ligand, facilitating the development of catalytic Sm(II) 5-<i>exo</i>-<i>trig </i>ketyl olefin cyclization reactions.



2019 ◽  
Vol 51 (3) ◽  
Author(s):  
Sajjad Moharramnejad ◽  
Omid Sofalian ◽  
Mostafa Valizadeh ◽  
Ali Asghari ◽  
Mohammad Reza Shiri ◽  
...  


1980 ◽  
Vol 45 (2) ◽  
pp. 369-375 ◽  
Author(s):  
Stanislav Miertuš ◽  
Ondrej Kyseľ

The 4-nitrobenzophenone radical anion prepared by electrolysis was studied by ESR spectroscopy. On the basis of the interpretation of ESR spectra, the conformation of this system was estimated. The effect of the concentration of supporting electrolyte and of the presence of a proton-donor agent (C2H5OH) was examined. It is assumed that changes in hyperfine splitting constants are caused by association.



2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Stephan Hirschi ◽  
David Kalbermatter ◽  
Zöhre Ucurum ◽  
Thomas Lemmin ◽  
Dimitrios Fotiadis

AbstractThe green-light absorbing proteorhodopsin (GPR) is the archetype of bacterial light-driven proton pumps. Here, we present the 2.9 Å cryo-EM structure of pentameric GPR, resolving important residues of the proton translocation pathway and the oligomerization interface. Superposition with the structure of a close GPR homolog and molecular dynamics simulations reveal conformational variations, which regulate the solvent access to the intra- and extracellular half channels harbouring the primary proton donor E109 and the proposed proton release group E143. We provide a mechanism for the structural rearrangements allowing hydration of the intracellular half channel, which are triggered by changing the protonation state of E109. Functional characterization of selected mutants demonstrates the importance of the molecular organization around E109 and E143 for GPR activity. Furthermore, we present evidence that helices involved in the stabilization of the protomer interfaces serve as scaffolds for facilitating the motion of the other helices. Combined with the more constrained dynamics of the pentamer compared to the monomer, these observations illustrate the previously demonstrated functional significance of GPR oligomerization. Overall, this work provides molecular insights into the structure, dynamics and function of the proteorhodopsin family that will benefit the large scientific community employing GPR as a model protein.



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