Monoselenophosphate: Synthesis, Characterization, and Identity with the Prokaryotic Biological Selenium Donor, Compound SePX

Richard S. Glass, Waheguru P. Singh, Woncheol Jung, Zsuzsa Veres, Thomas D. Scholz, Thressa C. Stadtman

Research output: Contribution to journalArticle

114 Scopus citations

Abstract

A labile, selenium donor compound required for synthesis of selenium-dependent enzymes and seleno-tRNAs is formed from ATP and selenide by the SELD enzyme. This compound, tentatively identified as a selenophosphate [Veres, Z., Tsai, L., Scholz, T. D., Politino, M., Balaban, R. S., & Stadtman, T. C. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2975–2979], is indistinguishable from chemically prepared monoselenophosphate by 31P NMR spectroscopy and ion pairing HPLC. Furthermore, addition of chemically prepared monoselenophosphate caused a dose-dependent decrease in the amount of 75Se incorporated into tRNAs from 75SePX generated in situ by SELD enzyme. A procedure is described for the chemical synthesis of monoselenophosphate in which the readily prepared (MeO)3PSe is converted in quantitative yield to (TMSO)3PSe followed by complete cleavage of the latter to monoselenophosphate in oxygen-free aqueous buffer. The chemical properties of chemically synthesized monoselenophosphate are described.

Original languageEnglish (US)
Pages (from-to)12555-12559
Number of pages5
JournalBiochemistry
Volume32
Issue number47
DOIs
StatePublished - Nov 30 1993

ASJC Scopus subject areas

  • Biochemistry

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