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

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

doi:10.1021/ja0317731

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

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

Chemistry

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	12833-12842
Number of pages	10
Journal	Journal of the American Chemical Society
Volume	126
Issue number	40
DOIs	https://doi.org/10.1021/ja0317731
State	Published - Oct 13 2004

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja0317731

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AU - Wilson, Andrew J.

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AB - 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.

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

Abstract

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