Redox-active films formed by electrochemical reduction of solutions of C60 and platinum complexes

2002 ◽  
Vol 12 (7) ◽  
pp. 2116-2122 ◽  
Author(s):  
Akari Hayashi ◽  
Ana de Bettencourt-Dias ◽  
Krzysztof Winkler ◽  
Alan L. Balch
Keyword(s):  
Electrochemical Reduction ◽  
Platinum Complexes ◽  
Redox Active

Redox-Active, Multinuclear (Ferrocenylethynyl)phosphanes and Their Palladium and Platinum Complexes

2006 ◽  
Vol 25 (23) ◽  
pp. 5657-5664 ◽  
Author(s):  
Thomas Baumgartner ◽  
Marcel Fiege ◽  
Florian Pontzen ◽  
Rocio Arteaga-Müller
Keyword(s):  
Platinum Complexes ◽  
Redox Active ◽  
Palladium And Platinum Complexes

Platinum complexes having redox-active PPh2CCFc and/or CCFc as terminal or bridging ligands

2009 ◽  
pp. 3434 ◽  
Author(s):  
Álvaro Díez ◽  
Elena Lalinde ◽  
M. Teresa Moreno ◽  
Sergio Sánchez
Keyword(s):  
Platinum Complexes ◽  
Bridging Ligands ◽  
Redox Active

Oleic acid peroxidation in the presence of metallo-porphyrins

2003 ◽  
Vol 07 (11) ◽  
pp. 719-724 ◽  
Author(s):  
Elena R. Milaeva ◽  
Yulia A. Gracheva ◽  
Dmitry B. Shpakovsky ◽  
Olga A. Gerasimova ◽  
Vladimir Yu. Tyurin ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Platinum Complexes ◽  
Inhibitory Effect ◽  
Radical Chain ◽  
Redox Active ◽  
Nickel Copper ◽  
Active Metal ◽  
Phenolic Group ◽  
Redox Active Metal

The influence of free bases of meso-tetrakis(3,5-di-tert-butyl-4-hydroxy-phenyl)porphyrins and meso-tetraphenylporphyrins and their complexes of Co , Ni , Cu , Pt upon the radical chain oxidation of oleic acid as model substrates for lipid peroxidation has been studied. It was shown that the introduction of the antioxidative phenolic fragment into the porphyrin ring leads to the dual activity of phenolic porphyrins when compared with their tetraphenyl substituted analogues in substrate oxidation. Free base phenolic porphyrins and their nickel, copper, platinum complexes demonstrate acute inhibitory effect upon oleic acid peroxidation due to the key role of 2,6-di-tert-butylphenol moities, whereas cobalt porphyrin exhibits dual activity associated with the presence of both the redox active metal center and phenolic group.

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.

In Situ X-Ray Absorption Studies of the Electrochemical Reduction of Hydroxocobalamin

1997 ◽  
Vol 7 (C2) ◽  
pp. C2-619-C2-620 ◽  
Author(s):  
M. Giorgett ◽  
I. Ascone ◽  
M. Berrettoni ◽  
S. Zamponi ◽  
R. Marassi
Keyword(s):  
Electrochemical Reduction ◽  
X Ray ◽  
Absorption Studies ◽  
X Ray Absorption
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