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

Kevin Groves, Andrew J. Wilson, Andrew 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
StatePublished - Oct 13 2004

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Metalloporphyrins
Proteolysis
Protein Conformation
Porphyrins
Cytochromes c
Dimers
Free energy
Conformations
Copper
Digestion
Peptide Hydrolases
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Catalytic unfolding and proteolysis of cytochrome c induced by synthetic binding agents. / Groves, Kevin; Wilson, Andrew J.; Hamilton, Andrew.

In: Journal of the American Chemical Society, Vol. 126, No. 40, 13.10.2004, p. 12833-12842.

Research output: Contribution to journalArticle

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