We have searched for sulfate-reducing bacteria in the feces of 41 healthy individuals and 110 patients from a Hepato-Gastro-Enterology Unit using a specific liquid medium (Test-kit Labège, Compagnie Française de Géothermie, Orléans, France). The 110 patients were separated in 22 patients presenting with inflammatory bowel diseases and 88 patients hospitalized for other lower (n=30) or upper (n=58) digestive tract diseases. Sulfate-reducing bacteria were isolated from 10 healthy individuals (24%), 15 patients presenting with inflammatory bowel diseases (68%), and 33 patients with other symptoms (37%). A multiplex PCR was devised for the identification of Desulfovibrio piger (formerly Desulfomonas pigra), Desulfovibrio fairfieldensis and Desulfovibrio desulfuricans, and applied to the above isolates. The strains of sulfate-reducing bacteria consisted of D. piger (39 isolates), D. fairfieldensis (19 isolates) and D. desulfuricans (one isolate). The prevalence of D. piger was significantly higher in inflammatory bowel disease patients (55%) as compared to healthy individuals (12%) or patients with other symptoms (25%) (P<0.05).

Solar-driven coupling of water oxidation with CO2 reduction sustains life on our planet and is of high priority in contemporary energy research. Here, we report a photoelectrochemical tandem device that performs photocatalytic reduction of CO2 to formate. We employ a semi-artificial design, which wires a W-dependent formate dehydrogenase (FDH) cathode to a photoanode containing the photosynthetic water oxidation enzyme, Photosystem II, via a synthetic dye with complementary light absorption. From a biological perspective, the system achieves a metabolically inaccessible pathway of light-driven CO2 fixation to formate. From a synthetic point of view, it represents a proof-of-principle system utilizing precious-metal-free catalysts for selective CO2-to-formate conversion using water as an electron donor. This hybrid platform demonstrates the translatability and versatility of coupling abiotic and biotic components to create challenging models for solar fuel and chemical synthesis.

Eight isolates of Desulfovibrio spp. have been obtained over 5 years from abdominal or brain abscesses or blood. In seven patients these strains were part of a mixed flora. One strain was isolated in pure culture from the blood of a patient with peritonitis of appendicular origin. According to the 16S rRNA gene sequences, this strain was close to Desulfovibrio fairfieldensis. The present report describes the fourth isolate of this recently described species to be isolated in pure culture or as a predominant part of the flora and to be associated with infectious processes. Thus, D. fairfieldensis may possess a higher pathogenic potential than other Desulfovibrio species.

Sulphate-reducing bacteria are important players in the global sulphur and carbon cycles, with considerable economical and ecological impact. However, the process of sulphate respiration is still incompletely understood. Several mechanisms of energy conservation have been proposed, but it is unclear how the different strategies contribute to the overall process. In order to obtain a deeper insight into the energy metabolism of sulphate-reducers whole-genome microarrays were used to compare

We describe the fabrication of gas diffusion electrodes modified with polymer/enzyme layers for electroenzymatic CO 2 fixation. For this, a metalfree organic low-potential viologen-modified polymer has been synthesized that reveals a redox potential of around −0.39 V vs SHE and is thus able to electrically wire W-dependent formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, which reversibly catalyzes the conversion of CO 2 to formate. The use of gas diffusion electrodes eliminates limitations arising from slow mass transport when solid carbonate is used as CO 2 source. The electrodes showed satisfactory stability that allowed for their long-term electrolysis application for electroenzymatic formate production.

The performance of heterogeneous catalysts for electrocatalytic CO 2 reduction (CO 2 R) suffers from unwanted side reactions and kinetic inefficiencies at the required large overpotential. However, immobilised CO 2 R enzymes — such as formate dehydrogenase — can operate with high turnover and selectivity at a minimal overpotential and are therefore ‘ideal’ model catalysts. Here, through the co-immobilisation of carbonic anhydrase, we study the effect of CO 2 hydration on the local environment and performance of a range of disparate CO 2 R systems from enzymatic (formate dehydrogenase) to heterogeneous systems. We show that the co-immobilisation of carbonic anhydrase increases the kinetics of CO 2 hydration at the electrode. This benefits enzymatic CO 2 reduction — despite the decrease in CO 2 concentration — due to a reduction in local pH change, whereas it is detrimental to heterogeneous catalysis (on Au), because the system is unable to suppress the H 2 evolution side reaction. Understanding the role of CO 2 hydration kinetics within the local environment on the performance of electrocatalyst systems provides important insights for the development of next generation synthetic CO 2 R catalysts.

Three membrane-bound redox complexes have been reported in Desulfovibrio spp., whose genes are not found in the genomes of other sulfate reducers such as Desulfotalea psycrophila and Archaeoglobus fulgidus. These complexes contain a periplasmic cytochrome c subunit of the cytochrome c(3) family, and their presence in these organisms probably correlates with the presence of a pool of periplasmic cytochromes c(3), also absent in the two other sulfate reducers. In this work we report the isolation and characterization of the first of such complexes, Tmc from D. vulgaris Hildenborough, which is associated with the tetraheme type II cytochrome c(3). The isolated Tmc complex contains four subunits, including the TpIIc(3) (TmcA), an integral membrane cytochrome b (TmcC), and two cytoplasmically predicted proteins, an iron-sulfur protein (TmcB) and a tryptophan-rich protein (TmcD). Spectroscopic studies indicate the presence of eight hemes c and two hemes b in the complex pointing to an alpha(2)betagammadelta composition (TmcA(2)BCD). EPR analysis reveals the presence of a [4Fe4S](3+) center and up to three other iron-sulfur centers in the cytoplasmic subunit. Nearly full reduction of the redox centers in the Tmc complex could be obtained upon incubation with hydrogenase/TpIc(3), supporting the role of this complex in transmembrane transfer of electrons resulting from periplasmic oxidation of hydrogen.

The growth characteristics, DNA G+C content and sequences of 16S rDNA and the transcribed 16S-23S rDNA internal spacer were determined for Desulfomonas pigra ATCC 29098T, Desulfovibrio desulfuricans subsp. desulfuricans strains Essex 6T (= ATCC 29577T) and MB (= ATCC 27774) and 'Desulfovibrio fairfieldensis' ATCC 700045. Despite phenotypic differences (shape and motility) between Desulfomonas pigra and Desulfovibrio strains, the molecular analysis suggests that Desulfomonas pigra should be reclassified within the genus Desulfovibrio. Thus, the reclassification is proposed of Desulfomonas pigra, the type and only species of the genus, as Desulfovibrio piger comb. nov., which implies the emendation of the description of the genus Desulfovibrio.