Cytochrome c as a peroxidase: tuning of heme reactivity

Author(s):
Diederix, R.E.M.
Published
2003
Publication type
Doctoral Thesis

Abstract

This thesis describes the peroxidase activity of the electron-transfer protein cytochrome c, and how it is controlled by the protein matrix. It is shown that unfolding cytochrome c has the effect to significantly enhance its peroxidase activity of (up to several thousand-fold). This can be achieved by chaotropic agents or by detergents. The hydrogen peroxide-driven inactivation of the heme cofactor of cytochrome c is also characterised.

Cytochrome cPeroxidaseProtein foldingHeme
Defense date
2003-05-21
Language
English
Supervisor(s)
Canters, G.W.
Advisor(s)
Ubbink, M.
Qualification
Ph.D.
Degree granting institution
Institute of Chemistry, Faculty of Science, Leiden University, Leiden
hdl
1887/4445

Juridical information

Court
LEI Universiteit Leiden

Funding

Sponsorship
Work supported by the Netherlands Research Council for Chemical Sciences (NWO-CW) with financial aid from the Netherlands Technology Foundation (STW), as part of the project ´Development of a new generation of heme-based mini-enzymes for cytochrome P450 and peroxidase-type conversions´ (STW project number WBI 3710).