Ditopic redox-active polyferrocenyl zinc(ii) dithiocarbamate macrocyclic receptors: synthesis, coordination and electrochemical recognition properties

2005 ◽  
pp. 774 ◽  
Author(s):  
Wallace W. H. Wong ◽  
David Curiel ◽  
Siu-Wai Lai ◽  
Michael G. B. Drew ◽  
Paul D. Beer
Keyword(s):  
Macrocyclic Receptors ◽  
Redox Active ◽  
Electrochemical Recognition

Redox Active Macrocyclic Receptors for Neutral Guests

2003 ◽  
Vol 42 (4) ◽  
pp. 1371-1377 ◽  
Author(s):  
Paul V. Bernhardt ◽  
Elizabeth J. Hayes
Keyword(s):  
Macrocyclic Receptors ◽  
Redox Active

Electrochemical recognition of group 1 and 2 metal cations by redox-active ionophores

1994 ◽  
Vol 225 (1-2) ◽  
pp. 137-144 ◽  
Author(s):  
Paul D. Beer ◽  
Zheng Chen ◽  
Michael G.B. Drew ◽  
Alexandra J. Pilgrim
Keyword(s):  
Metal Cations ◽  
Redox Active ◽  
Electrochemical Recognition ◽  
Group 1

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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