scholarly journals Proton Controlled Intramolecular Communication in Dinuclear Ruthenium(II) Polypyridine Complexes

2002 ◽  
Vol 41 (11) ◽  
pp. 2871-2878 ◽  
Author(s):  
Cinzia Di Pietro ◽  
Scolastica Serroni ◽  
Sebastiano Campagna ◽  
Maria Teresa Gandolfi ◽  
Roberto Ballardini ◽  
...  
Keyword(s):  
Dinuclear Ruthenium ◽  
Polypyridine Complexes ◽  
Intramolecular Communication

Mono- and Dinuclear Ruthenium(II) and Osmium(II) Polypyridine Complexes Built around Spiro-Bridged Bis(phenanthroline) Ligands: Synthesis, Electrochemistry, and Photophysics

2000 ◽  
Vol 39 (16) ◽  
pp. 3590-3598 ◽  
Author(s):  
Alberto Juris ◽  
Luca Prodi ◽  
Anthony Harriman ◽  
Raymond Ziessel ◽  
Muriel Hissler ◽  
...  
Keyword(s):  
Dinuclear Ruthenium ◽  
Polypyridine Complexes ◽  
Phenanthroline Ligands

Ruthenium Complexes for 1- and 2-Photon Photodynamic Therapy: From In Silico Prediction to In Vivo Applications

2020 ◽  
Author(s):  
Johannes Karges ◽  
Shi Kuang ◽  
Federica Maschietto ◽  
Olivier Blacque ◽  
Ilaria Ciofini ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
In Silico ◽  
Aqueous Solubility ◽  
The Body ◽  
Photon Absorption ◽  
Multicellular Tumor Spheroids ◽  
Spectral Window ◽  
Photon Excitation ◽  
Polypyridine Complexes

<div>The use of photodynamic therapy (PDT) against cancer has received increasing attention overthe recent years. However, the application of the currently approved photosensitizers (PSs) is somehow limited by their poor aqueous solubility, aggregation, photobleaching and slow clearance from the body. To overcome these limitations, there is a need for the development of new classes of PSs with ruthenium(II) polypyridine complexes currently gaining momentum. However, these compounds generally lack significant absorption in the biological spectral window, limiting their application to treat deep-seated or large tumors. To overcome this drawback, ruthenium(II) polypyridine complexes designed in silico with (E,E’)-4,4´-bisstyryl 2,2´-bipyridine ligands showed impressive 1- and 2-Photon absorption up to a magnitude higher than the ones published so far. While non-toxic in the dark, these compounds were found phototoxic in various 2D monolayer cells, 3D multicellular tumor spheroids and be able to eradicate a multiresistant tumor inside a mouse model upon clinically relevant 1-Photon and 2 Photon excitation.</div>

Hsp70 Escort Protein: More Than a Regulator of Mitochondrial Hsp70

2018 ◽  
Vol 16 (1) ◽  
pp. 64-73 ◽  
Author(s):  
David O. Nyakundi ◽  
Stephen J. Bentley ◽  
Aileen Boshoff
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Domain ◽  
C Terminus ◽  
Cellular Localisation ◽  
The Matrix ◽  
Mitochondrial Hsp70 ◽  
Cellular Compartments ◽  
Intramolecular Communication ◽  
Self Aggregation ◽  
J Protein

Hsp70 members occupy a central role in proteostasis and are found in different eukaryotic cellular compartments. The mitochondrial Hsp70/J-protein machinery performs multiple functions vital for the proper functioning of the mitochondria, including forming part of the import motor that transports proteins from the cytosol into the matrix and inner membrane, and subsequently folds these proteins in the mitochondria. However, unlike other Hsp70s, mitochondrial Hsp70 (mtHsp70) has the propensity to self-aggregate, accumulating as insoluble aggregates. The self-aggregation of mtHsp70 is caused by both interdomain and intramolecular communication within the ATPase and linker domains. Since mtHsp70 is unable to fold itself into an active conformation, it requires an Hsp70 escort protein (Hep) to both inhibit self-aggregation and promote the correct folding. Hep1 orthologues are present in the mitochondria of many eukaryotic cells but are absent in prokaryotes. Hep1 proteins are relatively small and contain a highly conserved zinc-finger domain with one tetracysteine motif that is essential for binding zinc ions and maintaining the function and solubility of the protein. The zinc-finger domain lies towards the C-terminus of Hep1 proteins, with very little conservation outside of this domain. Other than maintaining mtHsp70 in a functional state, Hep1 proteins play a variety of other roles in the cell and have been proposed to function as both chaperones and co-chaperones. The cellular localisation and some of the functions are often speculative and are not common to all Hep1 proteins analysed to date.

Revisiting Dinuclear Ruthenium Water Oxidation Catalysts: Effect of Bridging Ligand Architecture on Catalytic Activity

2021 ◽  
Vol 60 (3) ◽  
pp. 1806-1813
Author(s):  
Husain N. Kagalwala ◽  
Mahesh S. Deshmukh ◽  
Elamparuthi Ramasamy ◽  
Neelima Nair ◽  
Rongwei Zhou ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Water Oxidation ◽  
Oxidation Catalysts ◽  
Bridging Ligand ◽  
Dinuclear Ruthenium

Preparation of Coordinatively Asymmetrical Ruthenium(II) Polypyridine Complexes

1999 ◽  
Vol 38 (10) ◽  
pp. 2267-2278 ◽  
Author(s):  
Joseph A. Treadway ◽  
Thomas J. Meyer
Keyword(s):  
Polypyridine Complexes
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