Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme

Yogeet Kaur, Jesse Ybarra, Paul M. Horowitz

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Mutation of all nonessential cysteine residues to serines in rhodanese turns the enzyme into a form (C3S) that is fully active but less stable than wild type (WT). bis-ANS binding studies have shown that C3S has more hydrophobic exposure than WT, although both have similar secondary structures suggesting the flexibility of its structure. Activity of C3S falls once it binds bis-ANS, and covalent binding of bis-ANS to C3S is induced by light. bis-ANS binds to C3S in its C-terminal domain as is shown by gel electophoresis and proteolysis. bis-ANS binding makes the C-terminal domain more susceptible to trypsin cleavage.

Original languageEnglish (US)
Pages (from-to)255-261
Number of pages7
JournalProtein Journal
Volume23
Issue number4
DOIs
StatePublished - 2004
Externally publishedYes

Keywords

  • 4,4′-bis(1-anilino-8-napthalenesulfonic acid) (bis-ANS)
  • C3S
  • Rhodanese
  • Sulfhydryl groups

ASJC Scopus subject areas

  • Analytical Chemistry
  • Bioengineering
  • Biochemistry
  • Organic Chemistry

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