Different synthetic pathways of nanoparticle-cored dendrimers (NCDs): Effects on the properties and their application as redox active centers

2014 ◽  
Vol 52 (22) ◽  
pp. 3185-3197 ◽  
Author(s):  
Julieta I. Paez ◽  
Pablo Froimowicz ◽  
Katharina Landfester ◽  
Verónica Brunetti ◽  
Miriam Strumia
Keyword(s):  
1989 ◽  
Vol 264 (2) ◽  
pp. 735-744
Author(s):  
T Ohnishi ◽  
H Schägger ◽  
S W Meinhardt ◽  
R LoBrutto ◽  
T A Link ◽  
...  

2012 ◽  
Vol 18 (33) ◽  
pp. 10427-10435 ◽  
Author(s):  
Evangelos Krokos ◽  
Fabian Spänig ◽  
Michaela Ruppert ◽  
Andreas Hirsch ◽  
Dirk M. Guldi

2020 ◽  
Vol 56 (12) ◽  
pp. 1883-1886 ◽  
Author(s):  
Arijit Mallick ◽  
Hanfeng Liang ◽  
Osama Shekhah ◽  
Jiangtao Jia ◽  
Georges Mouchaham ◽  
...  

These predesigned Zr-based MOFs could pave the way for many applications related to supercapacitors.


2003 ◽  
Vol 75 (4) ◽  
pp. 461-481 ◽  
Author(s):  
D. Astruc

An overview of the metal-mediated synthesis and use of nanosized metallodendrimers is given with emphasis on electron-transfer processes (molecular batteries consisting in dendrimers decorated with a large number of equivalent redox-active centers) and catalytic reactions (electron-transfer-chain catalytic synthesis of dendrimers decorated with ruthenium carbonyl clusters, redox catalysis of nitrate and nitrite electroreduction in water by star-shape hexanuclear catalysts).


2021 ◽  
Vol 25 ◽  
Author(s):  
Alexis Prieto ◽  
Florian Jaroschik

: In recent years, photoredox catalysis has appeared as a new paradigm for forging a wide range of chemical bonds under mild conditions using abundant reagents. This approach allows many organic transformations through the generation of various radical species, enabling the valorization of non-traditional partners. A continuing interest has been devoted to the discovery of novel radical-generating procedures. Over the last ten years, strategies using rare-earth complexes as either redox-active centers or as redox-neutral Lewis acids have emerged. This review provides an overview of the recent accomplishments made in this field. It especially aims to demonstrate the utility of rare-earth complexes for ensuring photocatalytic transformations and to inspire future developments.


2019 ◽  
Vol 16 ◽  
pp. 236-242 ◽  
Author(s):  
Gaole Dai ◽  
Xuelan Wang ◽  
Yumin Qian ◽  
Zhihui Niu ◽  
Xi Zhu ◽  
...  

2020 ◽  
Vol 3 (1) ◽  
pp. 40
Author(s):  
Alexandra I. Costa ◽  
Patrícia D. Barata ◽  
José V. Prata

The sensing behavior of a calix[4]arene-oxacyclophane-carbazole conjugate (1) towards Cu(I) ions was investigated. Contrary to the noteworthy sensitivity and selectivity previously found for Cu(II), the affinity of 1 for Cu(I) cations is much lower. Through fluorescence titration assays, the apparent binding constants (Ka) for the two ions were determined, showing that an affinity of over thirteen fold was displayed for Cu(II). Two Cu(I) counter-ions were used to determine possible effects on the binding event. It was found that acetate and iodide ions behave similarly, yielding Ka of the same magnitude. Formation of a ground-state supramolecular complex between 1 and Cu(I) ions was not observed on UV-Vis titrations, in contrast to what was previously reported for Cu(II) using the same host. The affinity of 1 for Fe(III), a major biological competitor, was also assessed. The fluorescence of host 1 is quenched by Fe(III) ions although to a lesser extent (32% less efficient than Cu(II)). The study demonstrates that calixarene 1 is able to differentiate copper ions in two common oxidation states using fluorescence techniques, thereby suggesting its application for redox-active centers in biomimetic chemistry.


2021 ◽  
Vol 8 (11) ◽  
pp. 256-261
Author(s):  
Lars Kaduhr ◽  
Cindy Brachmann ◽  
Keerthiraju Ethiraju Ravichandran ◽  
James D. West ◽  
Sebastian Glatt ◽  
...  

Ubiquitin related modifier 1 (Urm1) is a unique eukaryotic member of the ubiquitin-fold (UbF) protein family and conserved from yeast to humans. Urm1 is dual-functional, acting both as a sulfur carrier for thiolation of tRNA anticodons and as a protein modifier in a lysine-directed Ub-like conjugation also known as urmylation. Although Urm1 conjugation coincides with oxidative stress and targets proteins like 2-Cys peroxiredoxins from yeast (Ahp1) and fly (Prx5), it was unclear how urmylation proceeds molecularly and whether it is affected by the activity of these antioxidant enzymes. An in-depth study of Ahp1 urmylation in yeast from our laboratory (Brachmann et al., 2020) uncovered that promiscuous lysine target sites and specific redox requirements determine the Urm1 acceptor activity of the peroxiredoxin. The results clearly show that the dimer interface and the 2-Cys based redox-active centers of Ahp1 are affecting the Urm1 conjugation reaction. Together with in vivo assays demonstrating that high organic peroxide concentrations can prevent Ahp1 from being urmylated, Brachmann et al. provide insights into a potential link between Urm1 utilization and oxidant defense of cells. Here, we highlight these major findings and discuss wider implications with regards to an emerging link between Urm1 conjugation and redox biology. Moreover, from these studies we propose to redefine our perspective on Urm1 and the molecular nature of urmylation, a post-translational conjugation that may not be that ubiquitin-like after all.


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