Desulfuromonas acetoxidans
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA35351 | ENA |
REPOSITORIES: ENA
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Project description:The solution structure of the three-heme electron transfer protein cytochrome c7 from Desulfuromonas acetoxidans is reported. The determination of the structure is obtained through NMR spectroscopy on the fully oxidized, paramagnetic form. The richness of structural motifs and the presence of three prosthetic groups in a protein of 68 residues is discussed in comparison with the four-heme cytochromes c3 already characterized through x-ray crystallography. In particular, the orientation of the three hemes present in cytochrome c7 is similar to that of three out of four hemes of cytochromes c3. The reduction potentials of the individual hemes, which have been obtained through the sequence-specific assignment of the heme resonances, are discussed with respect to the properties of the protein matrix. This information is relevant for any attempt to understand the electron transfer pathway.
| S-EPMC26143 | biostudies-literature
Project description:Multiheme cytochrome c proteins that belong to class III have been recently shown to exhibit a metal reductase activity, which could be of great environmental interest, especially in metal bioremediation. To get a better understanding of these activities, the gene encoding cytochrome c7 from the sulfur-reducing bacterium Desulfuromonas acetoxidans was cloned from genomic DNA by PCR and expressed in Desulfovibrio desulfuricans G201. The expression system was based on the cyc transcription unit from Desulfovibrio vulgaris Hildenborough and led to the synthesis of holocytochrome c7 when transferred by electrotransformation into the sulfate reducer Desulfovibrio desulfuricans G201. The produced cytochrome was indistinguishable from the protein purified from Desulfuromonas acetoxidans cells with respect to several biochemical and biophysical criteria and exhibited the same metal reductase activities as determined from electrochemical experiments. This suggests that the molecule was correctly folded in the host organism. Desulfovibrio desulfuricans produces functional multiheme c-type cytochromes from bacteria belonging to a different genus and may be considered a suitable host for the heterologous biogenesis of multiheme c-type cytochromes for either structural or engineering studies. This report, which presents the first example of the transformation of a Desulfovibrio desulfuricans strain by electrotransformation, describes work that is the first necessary step of a protein engineering program that aims to specify the structural features that are responsible for the metal reductase activities of multiheme cytochrome c7.
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Project description:Desulfatibacillum alkenivorans strain PF2803T, a mesophilic sulfur-reducing bacterium
2023-07-19 | MSV000092479 | MassIVE
Project description:Iron- and sulfur-reducing bacterium
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Project description: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.
2025-11-30 | PXD053556 | Pride