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André Gemünde, Nils‐Lennart Ruppert, Dirk Holtmann
This study elucidates mediated electron transfer (MET) mechanisms in Cupriavidus necator, a non-DET bacterium, using ferricyanide as a redox mediator in bioelectrochemical systems. Through inhibition studies, qPCR expression analysis, and deletion mutant experiments, cytochrome c oxidase (cbb3) was identified as the primary ferricyanide reduction site, with secondary involvement of nitrite reductase NirS. Outer membrane protein OmpA showed 2.9-fold upregulation under anodic conditions, suggesting a role in mediator uptake. Chemical membrane permeabilization doubled ferricyanide reduction rates, indicating membrane transport as a bottleneck for MET optimization.
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Abstract Cupriavidus necator , despite lacking direct electron transfer capabilities, demonstrates efficient reduction of various redox mediators in oxygen‐free cultivation within bioelectrochemical systems. This study investigates the reduction site of ferricyanide through inhibition and expression rate analysis of oxygen and nitrate respiration chain complexes, comparing aerobic cultivation conditions with fructose as carbon and electron donor to autotrophic (CO 2 /H 2 /O 2 ) and anodic cultivation conditions (fructose/anode). Azide inhibition identified cytochrome c oxidase as the primary complex facilitating electron transfer to ferricyanide, with a secondary role proposed for nitrite reductase NirS, demonstrating a 3.9±1.1‐fold higher expression when exposed to anodic conditions. The 2.9±0.6‐fold increase in the expression of the natural porin OmpA under anodic conditions implies its potential involvement in ferricyanide uptake. Additionally, chemically permeabilizing cell membranes with cetyltrimethylammonium bromide doubles ferricyanide reduction rates without an anode present, offering insights for optimizing redox mediation in C. necator based bioelectrochemical systems. This study opens up new possibilities for the targeted optimization of mediated electron transfer in C. necator and other organisms.