A study of dithiothreitol inactivation of the enzyme rhodanese

Seung K. Kim, Paul M. Horowitz

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

When air oxidized, partially inactivated rhodanese (EC 2.8.1.1) is treated with dithiothreitol (DTT) to regenerate the reduced essential sulfhydryl group there is an initial reactivation followed by an anomalous slower inactivation. Fully active enzyme shows only inactivation. The inactivated enzyme may be completely reactivated on long incubation with the substrate thiosulfate ion. None of the normal potentialities of DTT appear to be responsible for the inactivation. The results are interpreted in terms of disulfide formation between DTT and an essential enzymic sulfhydryl group with the resulting complex being stabilized by secondary interactions which are particularly favorable due to similarities between DTT and lipoic acid--a normal sulfur acceptor substrate.

Original languageEnglish (US)
Pages (from-to)433-439
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume67
Issue number1
DOIs
StatePublished - Nov 3 1975
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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