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Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site

Title data

di Savino, Antonella ; Förster, Johannes ; la Haye, Thijmen ; Blok, Anneloes ; Timmer, Monika ; Ullmann, G. Matthias ; Ubbink, Marcellus:
Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site.
In: Angewandte Chemie International Edition. Vol. 132 (2020) Issue 51 . - pp. 23439-23443.
ISSN 1521-3773
DOI: https://doi.org/10.1002/ange.202010006

Project information

Project title:
Project's official titleProject's id
SFB 1357 MikroplastikSFB1357

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

Electrostatic interactions can strongly increase the efficiency of protein complex formation. The charge distribution in redox proteins is often optimized to steer a redox partner to the electron transfer active binding site. To test whether the optimized distribution is more important than the strength of the electrostatic interactions, an additional negative patch was introduced on the surface of cytochrome c peroxidase, away from the stereospecific binding site, and its effect on the encounter complex as well as the rate of complex formation was determined. Monte Carlo simulations and paramagnetic relaxation enhancement NMR experiments indicate that the partner, cytochrome c, interacts with the new patch. Unexpectedly, the rate of the active complex formation was not reduced, but rather slightly increased. The findings support the idea that for efficient protein complex formation the strength of the electrostatic interaction is more critical than an optimized charge distribution.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Electrostatic interactions; Encounter complexes; NMR spectroscopy; Paramagnetic relaxation; Protein-protein interactions
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professor Bioinformatics/Structural Biology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professor Bioinformatics/Structural Biology > Professor Bioinformatics/Structural Biology - Univ.-Prof. Dr. Matthias Ullmann
Research Institutions > Collaborative Research Centers, Research Unit > SFB 1357 - MIKROPLASTIK
Faculties
Research Institutions
Research Institutions > Collaborative Research Centers, Research Unit
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 08 Feb 2021 08:10
Last Modified: 11 Mar 2021 06:34
URI: https://eref.uni-bayreuth.de/id/eprint/62808