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

Overview

Journal Angew Chem Int Ed Engl

Specialty Chemistry

Date 2020 Aug 23

PMID 32827196

Citations 6

Authors

Antonella Di Savino

Johannes M Foerster

Thijmen La Haye

Anneloes Blok

Monika Timmer

G Matthias Ullmann

Marcellus Ubbink

Affiliations

Soon will be listed here.

Abstract

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.

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