Catalytic unfolding and proteolysis of cytochrome c induced by synthetic binding agents

Kevin Groves, Andrew J. Wilson, Andrew D. Hamilton

Research output: Contribution to journalArticle

Abstract

A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibility of cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. The free energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol in the bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalent of metalloporphyrin to effect complete, rapid digestion in the presence of a protease.

Original languageEnglish (US)
Pages (from-to)12833-12842
Number of pages10
JournalJournal of the American Chemical Society
Volume126
Issue number40
DOIs
StatePublished - Oct 13 2004

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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