Reactivity and Redox Potential of Heme-Thiolate Proteins – Results from Enzymes and Enzyme Models

Authors

  • Wolf-D. Woggon Institute of Organic Chemistry, University of Basel, St. Johanns-Ring 19, CH-4056 Basel

DOI:

https://doi.org/10.2533/chimia.2001.366

Keywords:

Cytochrome p450, Enzymes, Enzyme models, Iron porphyrins, Iron-sulfonate coordination, Iron-thiolate coordination, Redox potential

Abstract

The redox potential is a characteristic parameter of various intermediates of the catalytic cycle of heme-thiolate proteins (cytochromes P450, NO-synthase, chloroperoxidase) which significantly influences catalytic turnover. E0 values of these proteins are surprisingly positive compared to synthetic active site analogues that have an arylthiolate or an alkylthiolate coordinating to the iron. This report examines factors underlying this phenomenon and describes the design of enzyme mimics having redox potentials close to those of heme-thiolate proteins.

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Published

2001-04-25

Issue

Vol. 55 No. 4 (2001): Chemical Biology / Biological Chemistry

Section

Scientific Articles

License

Copyright (c) 2001 Swiss Chemical Society

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

How to Cite

[1]
W.-D. Woggon, Chimia 2001, 55, 366, DOI: 10.2533/chimia.2001.366.