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

Antonella Di Savino, Johannes M. Foerster, Thijmen La Haye, Anneloes Blok, Monika Timmer, G. Matthias Ullmann, Marcellus Ubbink

    Research output: Contribution to journalArticleScientificpeer-review

    2 Citations (Scopus)
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    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.

    Original languageEnglish
    Pages (from-to)23239-23243
    Number of pages5
    JournalAngewandte Chemie - International Edition
    Volume59
    Issue number51
    DOIs
    Publication statusPublished - 2020

    Keywords

    • electrostatic interactions
    • encounter complexes
    • NMR spectroscopy
    • paramagnetic relaxation enhancement
    • protein–protein interactions

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