ArticleAngewandte Chemie (International ed. in English)2020
Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Discovery of an Antiviral Electron Transfer Process to Create Catalytically Self-Sufficient Viral Restriction Factors.Angewandte Chemie (International ed. in English) · 2026Article
- The regulatory potential of cytochrome P450-adrenodoxin interactions: Insights toward understanding redox partner regulation in drug metabolizing enzymes.Drug metabolism and disposition: the biological fate of chemicals · 2026Review
- Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide.NPJ Parkinson's disease · 2025Article
- Distinct association of HRAS and KRAS with MnMagnetic resonance letters · 2025Article
- Toward the Rational Design of Organic Catalysts for Organocatalysed Atom Transfer Radical Polymerisation.Polymers · 2024Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Preferential Interactions of a Crowder Protein with the Specific Binding Site of a Native Protein Complex.The journal of physical chemistry letters · 2022Article
- Enhancing the population of the encounter complex affects protein complex formation efficiency.The FEBS journal · 2022Article
- The Charge Distribution on a Protein Surface Determines Whether Productive or Futile Encounter Complexes Are Formed.Biochemistry · 2021Article
- Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site.Angewandte Chemie (International ed. in English) · 2020Article
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Authors and funding
7 authors.
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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.
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