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Desulfuromonas acetexigens full proteome

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NIAID Data Ecosystem2026-05-10 收录
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https://www.omicsdi.org/dataset/pride/PXD053556
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Desulfuromonas acetexigens is an anaerobic, Gram-negative bacterium capable of chemoorganotrophic growth on acetate as the energy and carbon source with elemental sulfur, fumarate, or malate as electron acceptors. D. acetexigens, first isolated from anoxic freshwater sediments, is a particularly interesting organism for studying extracellular electron transfer due to the ability to produce high current in a short amount of time. This ability could be attributed to several possible pathways, such as the porin-cytochrome-mediated or metal-reducing pathways, extensively studied in other organisms, such as Geobacter sulfurreducens and Schewanella oneidensis. Understanding the fundamentals of EET mechanisms coupled with the ongoing identification of novel organisms with EET capabilities is crucial for the advancement and optimization of microbial electrochemical technologies. These technologies hold remarkable potential for groundbreaking applications in bioremediation, biosensor development, and resource recovery operations. At present, a primary challenge holding back the scale-up and commercial viability of these applications is the relatively low efficiency of EET processes. Earlier sequenced genome allowed us to find genes related to the respective pathways, suggesting that D. acetexigens may use different pathways depending on the conditions. A previous study revealed that the redox potentials of EET-related proteins could be in the range from -0.5 V to +0.15 V vs. Ag/AgCl2. However, assessing whether the pathways are functional without comprehensive proteomics analysis is challenging. Here, we compared protein expression in biofilms grown under four different applied potentials to fumarate-grown planktonic culture using LC/MS2 operating in DIA mode. Further, we compared D. acetexigens proteins against G. sulfurreducens using PAW BLAST to better understand the function of less characterized proteins.
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2025-11-30
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