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. 1991 Apr 15;88(8):3057–3059. doi: 10.1073/pnas.88.8.3057

Metalloselenonein, the selenium analogue of metallothionein: synthesis and characterization of its complex with copper ions.

T Oikawa 1, N Esaki 1, H Tanaka 1, K Soda 1
PMCID: PMC51383  PMID: 1826562

Abstract

We used an automated peptide synthesizer to produce a peptide, metalloselenonein, that contains selenocysteine residues substituted for all cysteine residues in Neurospora crassa copper metallothionein. Metalloselenonein binds 3 mol of Cu(I) per mol. This adduct shows a broad absorption band between 230 and 400 nm and a fluorescence band at 395 nm, which can be attributed to copper-selenolate coordination. The circular dichroism spectrum of the copper-metalloselenonein complex shows a positive band around 245 nm attributable to asymmetry in metal coordination.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chocat P., Esaki N., Tanaka H., Soda K. Synthesis of L-selenodjenkolate and its degradation with methionine gamma-lyase. Anal Biochem. 1985 Aug 1;148(2):485–489. doi: 10.1016/0003-2697(85)90256-8. [DOI] [PubMed] [Google Scholar]
  2. Coch E. H., Greene R. C. The utilization of selenomethionine by Escherichia coli. Biochim Biophys Acta. 1971 Feb 23;230(2):223–236. doi: 10.1016/0304-4165(71)90207-8. [DOI] [PubMed] [Google Scholar]
  3. Cone J. E., Del Río R. M., Davis J. N., Stadtman T. C. Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety. Proc Natl Acad Sci U S A. 1976 Aug;73(8):2659–2663. doi: 10.1073/pnas.73.8.2659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Erickson B. W., Merrifield R. B. Use of chlorinated benzyloxycarbonyl protecting groups to eliminate N -branching at lysine during solid-phase peptide synthesis. J Am Chem Soc. 1973 May 30;95(11):3757–3763. doi: 10.1021/ja00792a047. [DOI] [PubMed] [Google Scholar]
  5. Fee J. A., Palmer G. The properties of parsley ferredoxin and its selenium-containing homolog. Biochim Biophys Acta. 1971 Aug 6;245(1):175–195. doi: 10.1016/0005-2728(71)90020-x. [DOI] [PubMed] [Google Scholar]
  6. Lerch K. Copper metallothionein, a copper-binding protein from Neurospora crassa. Nature. 1980 Mar 27;284(5754):368–370. doi: 10.1038/284368a0. [DOI] [PubMed] [Google Scholar]
  7. Merrifield B. Solid phase synthesis. Science. 1986 Apr 18;232(4748):341–347. doi: 10.1126/science.3961484. [DOI] [PubMed] [Google Scholar]
  8. Meyer J., Moulis J. M. Replacement of sulfide by selenide in the [4Fe-4S] clusters of the ferredoxin from Clostridium pasteurianum. Biochem Biophys Res Commun. 1981 Nov 30;103(2):667–673. doi: 10.1016/0006-291x(81)90502-7. [DOI] [PubMed] [Google Scholar]
  9. Mitchell A. R., Erickson B. W., Ryabtsev M. N., Hodges R. S., Merrifield R. B. Tert-butoxycarbonylaminoacyl-4-(oxymethyl)-phenylacetamidomethyl-resin, a more acid-resistant support for solid-phase peptide synthesis. J Am Chem Soc. 1976 Nov 10;98(23):7357–7362. doi: 10.1021/ja00439a041. [DOI] [PubMed] [Google Scholar]
  10. Sarin V. K., Kent S. B., Tam J. P., Merrifield R. B. Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction. Anal Biochem. 1981 Oct;117(1):147–157. doi: 10.1016/0003-2697(81)90704-1. [DOI] [PubMed] [Google Scholar]
  11. Stadtman T. C. Selenium-dependent enzymes. Annu Rev Biochem. 1980;49:93–110. doi: 10.1146/annurev.bi.49.070180.000521. [DOI] [PubMed] [Google Scholar]
  12. Theodoropoulos D., Schwartz I. L., Walter R. Synthesis of selenium-containing peptides. Biochemistry. 1967 Dec;6(12):3927–3932. doi: 10.1021/bi00864a039. [DOI] [PubMed] [Google Scholar]
  13. Walsh C. T., Schonbrunn A., Abeles R. H. Studies on the mechanism of action of D-amino acid oxidase. Evidence for removal of substrate -hydrogen as a proton. J Biol Chem. 1971 Nov 25;246(22):6855–6866. [PubMed] [Google Scholar]
  14. Walter R., Chan W. Y. Syntheses and pharmacological properties of selenium isologs of oxytocin and deamino-oxytocin. J Am Chem Soc. 1967 Jul 19;89(15):3892–3898. doi: 10.1021/ja00991a037. [DOI] [PubMed] [Google Scholar]
  15. Wilson G. S., Tsibris J. C., Gunsalus I. C. Electrochemical studies of putidaredoxin and its selenium analog. J Biol Chem. 1973 Sep 10;248(17):6059–6061. [PubMed] [Google Scholar]

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