The Role of a Complex Formation in the Dissolution of Iron Oxides in Orthophosphoric Acid

2021 ◽  
Vol 76 (6) ◽  
pp. 398-404
Author(s):  
A. V. Kuzin ◽  
I. G. Gorichev ◽  
V. A. Shelontsev ◽  
A. N. Kuzmenko ◽  
O. N. Plakhotnaia ◽  
...  
IUBMB Life ◽  
1997 ◽  
Vol 42 (4) ◽  
pp. 731-737 ◽  
Author(s):  
Yuriy Ivanov ◽  
Irina Kanaeva ◽  
Michail Eldarov ◽  
Konstantin Sklyabin ◽  
Michael Lehnerer ◽  
...  

2019 ◽  
Vol 351 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Dan Eude Kpannieu ◽  
Martine Mallet ◽  
Lacina Coulibaly ◽  
Mustapha Abdelmoula ◽  
Christian Ruby

Nanomaterials ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 9 ◽  
Author(s):  
Artiom Skripka ◽  
Dominyka Dapkute ◽  
Jurga Valanciunaite ◽  
Vitalijus Karabanovas ◽  
Ricardas Rotomskis

Nanomaterials have permeated various fields of scientific research, including that of biomedicine, as alternatives for disease diagnosis and therapy. Among different structures, quantum dots (QDs) have distinctive physico-chemical properties sought after in cancer research and eradication. Within the context of cancer therapy, QDs serve the role of transporters and energy donors to photodynamic therapy (PDT) drugs, extending the applicability and efficiency of classic PDT. In contrast to conventional PDT agents, QDs’ surface can be designed to promote cellular targeting and internalization, while their spectral properties enable better light harvesting and deep-tissue use. Here, we investigate the possibility of complex formation between different amphiphilic coating bearing QDs and photosensitizer chlorin e6 (Ce6). We show that complex formation dynamics are dependent on the type of coating—phospholipids or amphiphilic polymers—as well as on the surface charge of QDs. Förster’s resonant energy transfer occurred in every complex studied, confirming the possibility of indirect Ce6 excitation. Nonetheless, in vitro PDT activity was restricted only to negative charge bearing QD-Ce6 complexes, correlating with better accumulation in cancer cells. Overall, these findings help to better design such and similar complexes, as gained insights can be straightforwardly translated to other types of nanostructures—expanding the palette of possible therapeutic agents for cancer therapy.


2008 ◽  
Vol 75 (5) ◽  
pp. 1229-1235 ◽  
Author(s):  
Iman A. El Gheriany ◽  
Daniela Bocioaga ◽  
Anthony G. Hay ◽  
William C. Ghiorse ◽  
Michael L. Shuler ◽  
...  

ABSTRACT A common form of biocatalysis of Mn(II) oxidation results in the formation of biogenic Mn(III, IV) oxides and is a key reaction in the geochemical cycling of Mn. In this study, we grew the model Mn(II)-oxidizing bacterium Leptothrix discophora SS-1 in media with limited iron (0.1 μM iron/5.8 mM pyruvate) and sufficient iron (0.2 μM iron/5.8 mM pyruvate). The influence of iron on the rate of extracellular Mn(II) oxidation was evaluated. Cultures in which cell growth was limited by iron exhibited reduced abilities to oxidize Mn(II) compared to cultures in medium with sufficient iron. While the extracellular Mn(II)-oxidizing factor (MOF) is thought to be a putative multicopper oxidase, Mn(II) oxidation in the presence of zero added Cu(II) was detected and the decrease in the observed Mn(II) oxidation rate in iron-limited cultures was not relieved when the medium was supplemented with Cu(II). The decline of Mn(II) oxidation under iron-limited conditions was not accompanied by siderophore production and is unlikely to be an artifact of siderophore complex formation with Mn(III). The temporal variations in mofA gene transcript levels under conditions of limited and abundant iron were similar, indicating that iron limitation did not interfere with the transcription of the mofA gene. Our quantitative PCR results provide a step forward in understanding the regulation of Mn(II) oxidation. The mechanistic role of iron in Mn(II) oxidation is uncertain; the data are consistent with a direct requirement for iron as a component of the MOF or an indirect effect of iron resulting from the limitation of one of many cellular functions requiring iron.


Toxicon ◽  
2013 ◽  
Vol 74 ◽  
pp. 130-137 ◽  
Author(s):  
Kunat Suktham ◽  
Wanwarang Pathaichindachote ◽  
Boonhiang Promdonkoy ◽  
Chartchai Krittanai

Pancreatology ◽  
2017 ◽  
Vol 17 (3) ◽  
pp. S28
Author(s):  
Andrea Parniczky ◽  
Eszter Hegyi ◽  
Anna Zsófia Tóth ◽  
Ákos Szücs ◽  
Andrea Szentesi ◽  
...  

2018 ◽  
Vol 25 (18) ◽  
pp. 17797-17806 ◽  
Author(s):  
Buddhika Gunawardana ◽  
Peter J. Swedlund ◽  
Naresh Singhal ◽  
Michel K. Nieuwoudt
Keyword(s):  

2002 ◽  
Vol 115 (7) ◽  
pp. 1435-1440 ◽  
Author(s):  
Mickael Rialland ◽  
Francesco Sola ◽  
Corrado Santocanale

Formation of pre-replicative complexes at origins is an early cell cycle event essential for DNA duplication. A large body of evidence supports the notion that Cdc6 protein, through its interaction with the origin recognition complex, is required for pre-replicative complex assembly by loading minichromosome maintenance proteins onto DNA. In fission yeast and Xenopus, this reaction known as the licensing of chromatin for DNA replication also requires the newly identified Cdt1 protein. We studied the role of hCdt1 protein in the duplication of the human genome by antibody microinjection experiments and analyzed its expression during the cell cycle in human non-transformed cells. We show that hCdt1 is essential for DNA replication in intact human cells, that it executes its function in a window of the cell cycle overlapping with pre-replicative complex formation and that it is necessary for the loading of minichromosome maintenance proteins onto chromatin. Intriguingly, we observed that hCdt1 protein, in contrast to other licensing factors, is already present in serum-deprived G0 arrested cells and its levels increase only marginally upon re-entry in the cell cycle.


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