Unraveling the function in chlorite dismutases and related peroxidases by EPR
- Biotechnologie
Abstract
The heme b containing enzymes chlorite dismutase and dye-decolorizing peroxidase belong to the same protein superfamily. Despite their high structural similarity, their enzymatic activity is very different. Chlorite dismutase is capable of degrading the strong and toxic oxidant chlorite to chloride and dioxygen. In contrast, dye-decolorizing peroxidases are able to degrade a large variety of molecules, including textile dyes and lignin. This project aims at understanding which local structural elements in the heme environment govern the observed high variations in enzymatic functions. Two representative chlorite dismutases and two dye-decolorizing peroxidases will be recombinantly produced in E. coli and investigated by a broad set of biochemical and biophysical techniques available in the Belgian and Austrian laboratories. Importantly, advanced electron paramagnetic resonance spectroscopy in combination with protein engineering will be used as major tools to determine the local geometric and electronic structure of the heme site during the different steps in protein turnover. The same biophysical spectroscopic method will also be used to investigate the interaction of the enzymes with different heme-ligating molecules, such as substrates, ligands and inhibitors. Insight into the mechanistic working of the enzymes is essential in view of their potential technological applications, such as in bioremediation of the environmental pollutant chlorite or degradation of lignin in the transformation of biomass to biofuel.
www.icpp-spp.org
Project staff
Christian Obinger
Univ.Prof. Mag.rer.nat. Dr.rer.nat. Christian Obinger
christian.obinger@boku.ac.at
Tel: +43 1 47654-10011
Project Leader
01.02.2016 - 31.01.2019
BOKU partners
Funder
