cytochrome-c-t has been researched along with fumaric-acid* in 2 studies
2 other study(ies) available for cytochrome-c-t and fumaric-acid
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Influence of cytochrome charge and potential on the cathodic current of electroactive artificial biofilms.
An electroactive artificial biofilm has been optimized for the cathodic reduction of fumarate by Shewanella oneidensis. The system is based on the self-assembly of multi-walled carbon nanotubes with bacterial cells in the presence of a c-type cytochrome. The aggregates are then deposited on an electrode to form the electroactive artificial biofilm. Six c-type cytochromes have been studied, from bovine heart or Desulfuromonas and Desulfuvibrio strains. The isoelectric point of the cytochrome controls the self-assembly process that occurs only with positively-charged cytochromes. The redox potential of the cytochrome is critical for electron transfer reactions with membrane cytochromes of the Mtr pathway. Optimal results have been obtained with c Topics: Biofilms; Catalysis; Cytochromes c; Desulfovibrio vulgaris; Electrodes; Electron Transport; Fumarates; Isoelectric Point; Oxidation-Reduction; Static Electricity; Succinic Acid | 2018 |
Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble cytochromes.
Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c', and (6) a diheme bacterial cytochrome c peroxidase. These cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant as are the small tetraheme cytochrome and the tetraheme fumarate reductase. Published results on regulation of cytochromes from DNA microarrays and 2D-PAGE differ somewhat from our results, emphasizing the importance of multifaceted analyses in proteomics. Topics: Amino Acid Sequence; Cell Division; Cytochrome c Group; Cytochromes; Cytochromes c; Electrophoresis, Gel, Two-Dimensional; Fumarates; Genome, Bacterial; Heme; Molecular Sequence Data; Oligonucleotide Array Sequence Analysis; Proteome; Sequence Homology, Amino Acid; Shewanella; Spectrophotometry; Ultraviolet Rays | 2004 |