Selenium in chemistry and biochemistry in comparison to sulfur

@inproceedings{Wessjohann2007SeleniumIC,
  title={Selenium in chemistry and biochemistry in comparison to sulfur},
  author={Ludger A. Wessjohann and Alex R. Schneider and Muhammad Azeem Abbas and Wolfgang Brandt},
  booktitle={Biological chemistry},
  year={2007}
}
Abstract What makes selenoenzymes – seen from a chemist's view – so special that they cannot be substituted by just more analogous or adapted sulfur proteins? This review compiles and compares physicochemical properties of selenium and sulfur, synthetic routes to selenocysteine (Sec) and its peptides, and comparative studies of relevant thiols and selenols and their (mixed) dichalcogens, required to understand the special role of selenium in selenoproteins on the atomic molecular level. The… 

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References

SHOWING 1-10 OF 147 REFERENCES
Sulfur and selenium: the role of oxidation state in protein structure and function.
TLDR
It is apparent that the chalcogen amino acids cysteine, methionine, selenocysteines, and selenomethionine exhibit a unique biological chemistry that is the source of exciting research opportunities.
Isosteric replacement of sulfur with other chalcogens in peptides and proteins
  • L. Moroder
  • Chemistry, Biology
    Journal of peptide science : an official publication of the European Peptide Society
  • 2005
The review addresses the functional and structural properties of the two series of chalcogen analogues of amino acids in peptides and proteins, the methionine and the serine/cysteine series, and
Selenoprotein synthesis: UGA does not end the story.
Active sites of thioredoxin reductases: Why selenoproteins?
TLDR
It is shown that the serine residues flanking the C-terminal Cys residues of Drosophila TrxRs are responsible for activating the cysteines to match the catalytic efficiency of a selenocysteine-cysteine pair as in mammalian TrxR, obviating the need for selenium.
Selenium metabolism in micro-organisms.
Recent developments in selenium metabolism and chemical speciation: a review.
  • S. G. Patching, P. Gardiner
  • Biology, Chemistry
    Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements
  • 1999
Glutathione peroxidase revisited--simulation of the catalytic cycle by computer-assisted molecular modelling.
TLDR
Comparison of molecular models of GPX with those of other members of the GPX superfamily reveals that the cosubstrate binding mechanisms are unique for the classical type of cytosolic glutathione peroxidases but cannot operate e.
Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety.
TLDR
A small, heat-stable selenoprotein, one of the components of the glycine reductase complex, was labeled with 75Se by growth of Clostridium sticklandii in the presence of Na2 75SeO3 and the selenium-containing moiety was shown to be a selenocysteine residue.
Selenocysteine: the 21st amino acid
TLDR
The aim of this article is to review the events leading to the elucidation of selenocysteine as being the 21st amino acid.
...
1
2
3
4
5
...