Thieno[3,2‐ b ]Thiophene End‐Capped all‐Sulfur Analog of 3,4‐Ethylenedioxythiophene and its Eletrosynthesized Polymer: Is Distorted Conformation Not Suitable for Electrochromism?

2019 ◽  
Vol 57 (10) ◽  
pp. 1041-1048 ◽  
Author(s):  
Yu Xue ◽  
Zexu Xue ◽  
Wenwen Zhang ◽  
Wenna Zhang ◽  
Shuai Chen ◽  
...  
Keyword(s):  
Sulfur Analog

Coordination chemistry of the sulfur analog of tricatechol siderophores

2009 ◽  
pp. 7350 ◽  
Author(s):  
Birgit Birkmann ◽  
Wolfram W. Seidel ◽  
Tania Pape ◽  
Andreas W. Ehlers ◽  
Koop Lammertsma ◽  
...  
Keyword(s):  
Coordination Chemistry ◽  
Sulfur Analog

cis-syn Photodimer of 1-thiauracil. Sulfur analog of the cis-syn photodimer of uracil

1971 ◽  
Vol 93 (18) ◽  
pp. 4574-4579 ◽  
Author(s):  
Elinor Adman ◽  
J. B. Bremner ◽  
R. N. Warrener ◽  
L. H. Jensen
Keyword(s):  
Sulfur Analog

ChemInform Abstract: A Novel Synthesis of the Sulfur Analog of Δ6-PGI1.

1982 ◽  
Vol 13 (37) ◽  
Author(s):  
H. YOKOMORI ◽  
Y. TORISAWA ◽  
M. SHIBASAKI ◽  
S. IKEGAMI
Keyword(s):  
Novel Synthesis ◽  
Sulfur Analog

scholarly journals EnzymicN-acetylation of a sulfur analog of L-lysine,S-(β-aminoethyl)-L-cysteine

FEBS Letters ◽  
1970 ◽  
Vol 8 (5) ◽  
pp. 301-303 ◽  
Author(s):  
K. Soda ◽  
H. Tanaka ◽  
T. Yamamoto
Keyword(s):  
Sulfur Analog

A Novel Synthesis of the Sulfur Analog of ∆6-PGI1

Heterocycles ◽  
1982 ◽  
Vol 18 (1) ◽  
pp. 251 ◽  
Author(s):  
Shiro Ikegami ◽  
Hiroko Yokomori ◽  
Yasuhiro Torisawa ◽  
Masakatsu Shibasaki
Keyword(s):  
Novel Synthesis ◽  
Sulfur Analog

scholarly journals Selenomethionine: A Pink Trojan Redox Horse with Implications in Aging and Various Age-Related Diseases

Antioxidants ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 882
Author(s):  
Muhammad Jawad Nasim ◽  
Mhd Mouayad Zuraik ◽  
Ahmad Yaman Abdin ◽  
Yannick Ney ◽  
Claus Jacob
Keyword(s):  
Mammalian Cells ◽  
Active Metabolites ◽  
Selenium Compounds ◽  
Redox Biology ◽  
Physiological Conditions ◽  
Organic Selenium ◽  
Age Related ◽  
Redox Active ◽  
Aging Health ◽  
Sulfur Analog

Selenium is an essential trace element. Although this chalcogen forms a wide variety of compounds, there are surprisingly few small-molecule organic selenium compounds (OSeCs) in biology. Besides its more prominent relative selenocysteine (SeCys), the amino acid selenomethionine (SeMet) is one example. SeMet is synthesized in plants and some fungi and, via nutrition, finds its way into mammalian cells. In contrast to its sulfur analog methionine (Met), SeMet is extraordinarily redox active under physiological conditions and via its catalytic selenide (RSeR’)/selenoxide (RSe(O)R’) couple provides protection against reactive oxygen species (ROS) and other possibly harmful oxidants. In contrast to SeCys, which is incorporated via an eloquent ribosomal mechanism, SeMet can enter such biomolecules by simply replacing proteinogenic Met. Interestingly, eukaryotes, such as yeast and mammals, also metabolize SeMet to a small family of reactive selenium species (RSeS). Together, SeMet, proteins containing SeMet and metabolites of SeMet form a powerful triad of redox-active metabolites with a plethora of biological implications. In any case, SeMet and its family of natural RSeS provide plenty of opportunities for studies in the fields of nutrition, aging, health and redox biology.

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