scholarly journals Redox-Active Guanidines with One or Two Guanidino Groups and Their Integration in Low-Dimensional Perovskite Structures

2019 ◽  
Vol 2019 (38) ◽  
pp. 4147-4160 ◽  
Author(s):  
Petra Walter ◽  
Elisabeth Kaifer ◽  
Hendrik Herrmann ◽  
Hubert Wadepohl ◽  
Olaf Hübner ◽  
...  
Keyword(s):  
Redox Active ◽  
Low Dimensional

Incorporation of a Redox-Active Bis(guanidine) in Low-Dimensional Tin and Lead Iodide Structures

2017 ◽  
Vol 2017 (47) ◽  
pp. 5539-5544 ◽  
Author(s):  
Hendrik Herrmann ◽  
Petra Walter ◽  
Elisabeth Kaifer ◽  
Hans-Jörg Himmel
Keyword(s):  
Lead Iodide ◽  
Redox Active ◽  
Low Dimensional

scholarly journals Front Cover: Incorporation of a Redox-Active Bis(guanidine) in Low-Dimensional Tin and Lead Iodide Structures (Eur. J. Inorg. Chem. 47/2017)

2017 ◽  
Vol 2017 (47) ◽  
pp. 5536-5536
Author(s):  
Hendrik Herrmann ◽  
Petra Walter ◽  
Elisabeth Kaifer ◽  
Hans-Jörg Himmel
Keyword(s):  
Lead Iodide ◽  
Front Cover ◽  
Redox Active ◽  
Low Dimensional

scholarly journals Ultrasensitive Materials for Electrochemical Biosensor Labels

Sensors ◽  
2020 ◽  
Vol 21 (1) ◽  
pp. 89
Author(s):  
Aneesh Koyappayil ◽  
Min-Ho Lee
Keyword(s):  
Carbon Materials ◽  
Electrochemical Biosensor ◽  
Electrochemical Techniques ◽  
Label Free ◽  
The Past ◽  
Redox Active ◽  
Sensitive Determination ◽  
Detection Of Biomolecules ◽  
Low Dimensional

Since the fabrication of the first electrochemical biosensor by Leland C. Clark in 1956, various labeled and label-free sensors have been reported for the detection of biomolecules. Labels such as nanoparticles, enzymes, Quantum dots, redox-active molecules, low dimensional carbon materials, etc. have been employed for the detection of biomolecules. Because of the absence of cross-reaction and highly selective detection, labeled biosensors are advantageous and preferred over label-free biosensors. The biosensors with labels depend mainly on optical, magnetic, electrical, and mechanical principles. Labels combined with electrochemical techniques resulted in the selective and sensitive determination of biomolecules. The present review focuses on categorizing the advancement and advantages of different labeling methods applied simultaneously with the electrochemical techniques in the past few decades.

scholarly journals Incorporation of a Redox-Active Bis(guanidine) in Low-Dimensional Tin and Lead Iodide Structures

2017 ◽  
Vol 2017 (47) ◽  
pp. 5537-5537
Author(s):  
Hendrik Herrmann ◽  
Petra Walter ◽  
Elisabeth Kaifer ◽  
Hans-Jörg Himmel
Keyword(s):  
Lead Iodide ◽  
Redox Active ◽  
Low Dimensional

scholarly journals MOFs based on 1D structural sub-domains with Brønsted acid and redox active sites as effective bi-functional catalysts

2020 ◽  
Vol 10 (11) ◽  
pp. 3572-3585 ◽  
Author(s):  
José María Moreno ◽  
Alexandra Velty ◽  
Urbano Díaz
Keyword(s):  
Active Sites ◽  
Bronsted Acid ◽  
Brønsted Acid ◽  
One Pot ◽  
Redox Active ◽  
Brönsted Acid ◽  
Low Dimensional

Low-dimensional MOF-type catalysts containing Brønsted acid and redox active sites, based on assembled 1D organic–inorganic nanoribbons, for one-pot two-step reactions.

Common modifications of selenocysteine in selenoproteins

2019 ◽  
Vol 64 (1) ◽  
pp. 45-53 ◽  
Author(s):  
Elias S.J. Arnér
Keyword(s):  
Amino Acids ◽  
Covalent Binding ◽  
Physicochemical Characteristics ◽  
Redox Active

Abstract Selenocysteine (Sec), the sulfur-to-selenium substituted variant of cysteine (Cys), is the defining entity of selenoproteins. These are naturally expressed in many diverse organisms and constitute a unique class of proteins. As a result of the physicochemical characteristics of selenium when compared with sulfur, Sec is typically more reactive than Cys while participating in similar reactions, and there are also some qualitative differences in the reactivities between the two amino acids. This minireview discusses the types of modifications of Sec in selenoproteins that have thus far been experimentally validated. These modifications include direct covalent binding through the Se atom of Sec to other chalcogen atoms (S, O and Se) as present in redox active molecular motifs, derivatization of Sec via the direct covalent binding to non-chalcogen elements (Ni, Mb, N, Au and C), and the loss of Se from Sec resulting in formation of dehydroalanine. To understand the nature of these Sec modifications is crucial for an understanding of selenoprotein reactivities in biological, physiological and pathophysiological contexts.

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