ArticleAngewandte Chemie (International ed. in English)2018
Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The pH-dependence of copper(ii/i) reduction potentials in variants ofRSC advances · 2026Article
- The Influence of pH on Long-Range Electron Transfer and Proton-Coupled Electron Transfer in Ruthenium-Modified Azurin.Molecules (Basel, Switzerland) · 2025Article
- An Investigation of the Influence of Tyrosine Local Interactions on Electron Hopping in a Model Protein.Molecules (Basel, Switzerland) · 2024Article
- Charge Regulation in a Rieske Proton Pump Pinpoints Zero, One, and Two Proton-Coupled Electron Transfer.Journal of the American Chemical Society · 2023Article
- Cofactor Dynamics Couples the Protein Surface to the Heme in CytochromeThe journal of physical chemistry. B · 2022Article
- Free Energies of Proton-Coupled Electron Transfer Reagents and Their Applications.Chemical reviews · 2022Review
- Measuring how two proteins affect each other's net charge in a crowded environment.Protein science : a publication of the Protein Society · 2021Article
- Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer.Angewandte Chemie (International ed. in English) · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Determining whether a protein regulates its net electrostatic charge during electron transfer (ET) will deepen our mechanistic understanding of how polypeptides tune rates and free energies of ET (e.g., by affecting reorganization energy, and/or redox potential). Charge regulation during ET has never been measured for proteins because few tools exist to measure the net charge of a folded protein in solution at different oxidation states. Herein, we used a niche analytical tool (protein charge ladders analyzed with capillary electrophoresis) to determine that the net charges of myoglobin, cytochrome c, and azurin change by 0.62±0.06, 1.19±0.02, and 0.51±0.04 units upon single ET. Computational analysis predicts that these fluctuations in charge arise from changes in the pK
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