ArticleProtein science : a publication of the Protein Society2023
Characterization of the inner membrane cytochrome ImcH from Geobacter reveals its importance for extracellular electron transfer and energy conservation.
Article in Protein science : a publication of the Protein Society, 2023. 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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10 citing papers in PubMed, 19 citations in OpenAlex.
- Overview of pathways and dynamic interactions of c-type cytochromes in Geobacter sulfurreducens.Biochemical Society transactions · 2026Review
- Ghost-rocks' microbiota: metagenomic insights into their influence on the biogeochemistry of karstic cave and groundwater.FEMS microbiology ecology · 2026Article
- Cross-scale design of abiotic-biotic interfaces for semi-artificial photosynthesis.Chemical science · 2026Review
- Decoupled respiration in electro-active bacteria.Communications biology · 2025Article
- Electron transport across the cell envelope via multihemeFrontiers in chemistry · 2025Review
- A survey of the Desulfuromonadia "cytochromome" provides a glimpse of the unexplored diversity of multiheme cytochromes in nature.BMC genomics · 2024Article
- Isolation and genomic analysis of "Applied and environmental microbiology · 2024Article
- Engineering of bespoke photosensitiser-microbe interfaces for enhanced semi-artificial photosynthesis.Chemical science · 2024Review
- Periplasmic electron transfer network in Geobacter sulfurreducens revealed by biomolecular interaction studies.Protein science : a publication of the Protein Society · 2024Article
- Characterization of the inner membrane cytochrome ImcH from Geobacter reveals its importance for extracellular electron transfer and energy conservation.Protein science : a publication of the Protein Society · 2023Article
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8 authors at 3 institutions in 2 countries.
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Abstract
Electroactive bacteria combine the oxidation of carbon substrates with an extracellular electron transfer (EET) process that discharges electrons to an electron acceptor outside the cell. This process involves electron transfer through consecutive redox proteins that efficiently connect the inner membrane to the cell exterior. In this study, we isolated and characterized the quinone-interacting membrane cytochrome c ImcH from Geobacter sulfurreducens, which is involved in the EET process to high redox potential acceptors. Spectroscopic and electrochemical studies show that ImcH hemes have low midpoint redox potentials, ranging from -150 to -358 mV, and connect the oxidation of the quinol-pool to EET, transferring electrons to the highly abundant periplasmic cytochrome PpcA with higher affinity than to its homologues. Despite the larger number of hemes and transmembrane helices, the ImcH structural model has similarities with the NapC/NirT/NrfH superfamily, namely the presence of a quinone-binding site on the P-side of the membrane. In addition, the first heme, likely involved on the quinol oxidation, has apparently an unusual His/Gln coordination. Our work suggests that ImcH is electroneutral and transfers electrons and protons to the same side of the membrane, contributing to the maintenance of a proton motive force and playing a central role in recycling the menaquinone pool.
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