ArticleSmall (Weinheim an der Bergstrasse, Germany)2025
Long-Distance Charge Transport between Cytochrome c and Complex III is Mediated by Protons and Reactive Oxygen Species.
Article in Small (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Quantifying the Characteristic Turnover Frequency of an Individual Redox Enzyme via Real-Time Electrical Transduction of Catalytic Events in a Label-Free Single-Protein Junction.Journal of the American Chemical Society · 2026Article
- Long-Distance Charge Transport between Cytochrome c and Complex III is Mediated by Protons and Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Electron transfer (ET) between redox proteins is an essential process in the respiratory and photosynthetic transport chains. While intra-protein ET is well characterized, the experimental methods to investigate inter-protein ET are limited by the presence of the solvent and by the transient nature of the protein-protein interaction and ET event, which are averaged in protein ensembles. Wiring precisely oriented redox protein partners to the nanoscale electrodes of an electrochemical scanning tunneling microscope allows recording the time- and distance-dependence of the current flowing between them. These methods have revealed that the current flowing between individual protein pairs extends beyond tunneling distances and that it is electrochemically gated. However, the corresponding mechanism and the identity of the charge carriers in aqueous solution remain to be elucidated. To determine the species involved in long-distance charge transport between the redox partner proteins Cc and Cc
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