Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. 1976 Aug; 73(8): 2659–2663.
PMCID: PMC430707

Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety.


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. The selenium-containing moiety, which is essential for the biological activity of the protein, was shown to be a selenocysteine residue. It was isolated as its Se-carboxymethyl, Se-carboxyethyl, and Se-aminoethyl derivatives from digests of the pure 75Se-labeled protein that had been reduced and treated with the various alkylating agents prior to hydrolysis. In each instance the 75Se-labeled moiety obtained from an alkylated protein sample and the corresponding alkyl derivative of authentic selenocysteine were indistinguishable. Several studies of the native selenoprotein detected a chromophore (UVmax 238nm) that appeared upon reduction of the protein with KBH4 and rapidly disappeared upon exposure to oxygen. This oxygen-labile chromophore is thought to be the ionized -SeH group of the selenocysteine residue.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (960K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Stadtman TC. Glycine reduction to acetate and ammonia: identification of ferredoxin and another low molecular weight acidic protein as components of the reductase system. Arch Biochem Biophys. 1966 Jan;113(1):9–19. [PubMed]
  • Turner DC, Stadtman TC. Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein. Arch Biochem Biophys. 1973 Jan;154(1):366–381. [PubMed]
  • Stadtman TC. Selenium biochemistry. Science. 1974 Mar 8;183(4128):915–922. [PubMed]
  • Oh SH, Ganther HE, Hoekstra WG. Selenium as a component of glutathione periodase isolated from ovine erythrocytes. Biochemistry. 1974 Apr 23;13(9):1825–1829. [PubMed]
  • Noguchi T, Cantor AH, Scott ML. Mode of action of selenium and vitamin E in prevention of exudative diathesis in chicks. J Nutr. 1973 Oct;103(10):1502–1511. [PubMed]
  • PINSENT J. The need for selenite and molybdate in the formation of formic dehydrogenase by members of the coli-aerogenes group of bacteria. Biochem J. 1954 May;57(1):10–16. [PMC free article] [PubMed]
  • Lester RL, DeMoss JA. Effects of molybdate and selenite on formate and nitrate metabolism in Escherichia coli. J Bacteriol. 1971 Mar;105(3):1006–1014. [PMC free article] [PubMed]
  • Enoch HG, Lester RL. The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. J Biol Chem. 1975 Sep 10;250(17):6693–6705. [PubMed]
  • Andreesen JR, Ljungdahl LG. Formate dehydrogenase of Clostridium thermoaceticum: incorporation of selenium-75, and the effects of selenite, molybdate, and tungstate on the enzyme. J Bacteriol. 1973 Nov;116(2):867–873. [PMC free article] [PubMed]
  • Heizmann CW, Malencik DA, Fischer EH. Generation of parvalbumin-like proteins from troponin. Biochem Biophys Res Commun. 1974 Mar 15;57(1):162–168. [PubMed]
  • Greaser ML, Gergely J. Purification and properties of the components from troponin. J Biol Chem. 1973 Mar 25;248(6):2125–2133. [PubMed]
  • Huber RE, Criddle RS. Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs. Arch Biochem Biophys. 1967 Oct;122(1):164–173. [PubMed]
  • ROSEN H. A modified ninhydrin colorimetric analysis for amino acids. Arch Biochem Biophys. 1957 Mar;67(1):10–15. [PubMed]
  • Takahashi K. Products of performic acid oxidation and acid hydrolysis of S-carboxymethylcysteine and related compounds. J Biochem. 1973 Dec;74(6):1083–1089. [PubMed]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences


Save items

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


  • Cited in Books
    Cited in Books
    PubMed Central articles cited in books
  • Compound
    PubChem Compound links
  • MedGen
    Related information in MedGen
  • PubMed
    PubMed citations for these articles
  • Substance
    PubChem Substance links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...