Growth of Sulphate-reducing Bacteria by Fumarate Dismutation

Miller, Jonathan D.; Wakerley, D. S.

doi:10.1099/00221287-43-1-101

Cited by 50 publications

(14 citation statements)

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“…Growth on fumarate (Miller and Wakerley 1966) and malate (Miller et al 1970) was already reported for various Desulfovibrio strains. For each fumarate oxidized to acetate via malate and pyruvate, two fumarate molecules are reduced to succinate (Hatchikian and Le Gall 1970a, b;Hatchikian 1972).…”

Section: Discussionmentioning

confidence: 53%

Characterization of Desulfovibrio fructosovorans sp. nov.

Ollivier¹,

et al. 1988

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Abstract. Desulfovibrio strain JJ isolated from estuarine sediment differed from all other described Desulfovibrio species by the ability to degrade fructose. The oxidation was incomplete, leading to acetate production. Fructose, malate and fumarate were fermented mainly to succinate and acetate in the absence of an external electron acceptor. The pH and temperature optima for growth were 7.0 and 35°C respectively. Strain JJ was motile by means of a single polar flagellum. The DNA base composition was 64.13% G S C . Cytochrome c3 and desulfoviridin were present. These characteristics established the isolate as a new species of the genus Desulfovibrio, and the name Desulfovibrio fiuctosovorans is proposed.

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Section: Discussionmentioning

confidence: 53%

Characterization of Desulfovibrio fructosovorans sp. nov.

Ollivier¹,

et al. 1988

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“…Malic enzyme, fumarase and acetate kinase were demonstrated also by their enzymic activities (Lewis & Miller, 1977;Brown & Akagi, 1966). Malate, which was suggested earlier as a product of fumarate disproportionation (Miller & Wakerley, 1966), apparently is only an intermediate. A similar form of fumarate disproportionation with succinate, acetate and CO 2 as the products was described for Clostridium formicoaceticum (Dorn et al, 1978), whereas fumarate disproportionation by Proteus rettgeri produced only succinate but no acetate (Kröger, 1974).…”

Section: Discussion Fumarate Respiration and Disproportionation By Sumentioning

confidence: 80%

Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria

et al. 2006

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Sulphate-or sulphur-reducing bacteria with known or draft genome sequences (Desulfovibrio vulgaris, Desulfovibrio desulfuricans G20, Desulfobacterium autotrophicum [draft], Desulfotalea psychrophila and Geobacter sulfurreducens) all contain sdhCAB or frdCAB gene clusters encoding succinate : quinone oxidoreductases. frdD or sdhD genes are missing. The presence and function of succinate dehydrogenase versus fumarate reductase was studied. Desulfovibrio desulfuricans (strain Essex 6) grew by fumarate respiration or by fumarate disproportionation, and contained fumarate reductase activity. Desulfovibrio vulgaris lacked fumarate respiration and contained succinate dehydrogenase activity. Succinate oxidation by the menaquinone analogue 2,3-dimethyl-1,4-naphthoquinone depended on a proton potential, and the activity was lost after degradation of the proton potential. The membrane anchor SdhC contains four conserved His residues which are known as the ligands for two haem B residues. The properties are very similar to succinate dehydrogenase of the Gram-positive (menaquinone-containing) Bacillus subtilis, which uses a reverse redox loop mechanism in succinate : menaquinone reduction. It is concluded that succinate dehydrogenases from menaquinone-containing bacteria generally require a proton potential to drive the endergonic succinate oxidation. Sequence comparison shows that the SdhC subunit of this type lacks a Glu residue in transmembrane helix IV, which is part of the uncoupling E-pathway in most non-electrogenic FrdABC enzymes.

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“…Since C 4 compounds of the reductive TCA branch did not accumulate in I2 cultures, regardless of growth mode or electron donor (Table 2), we considered that I2 had altered fumarate metabolism. The growth of SRB by fumarate disproportionation has been described previously (53), where 3 fumarate ¡ 1 acetate ϩ 2 succinate ϩ 2 CO 2 . When G20 grown in lactate-sulfate was inoculated into fumarate medium, robust growth occurred after a lag (data not shown) and the expected primary end products of succinate and acetate accumulated in the predicted 2:1 ratio as the cells entered stationary phase (data not shown).…”

Section: Resultsmentioning

confidence: 99%

New Model for Electron Flow for Sulfate Reduction in Desulfovibrio alaskensis G20

Keller

Rapp-Giles

Semkiw

et al. 2014

Appl Environ Microbiol

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To understand the energy conversion activities of the anaerobic sulfate-reducing bacteria, it is necessary to identify the components involved in electron flow. The importance of the abundant type I tetraheme cytochrome c 3 (TpIc 3 ) as an electron carrier during sulfate respiration was questioned by the previous isolation of a null mutation in the gene encoding TpIc 3 , cycA, in Desulfovibrio alaskensis G20. Whereas respiratory growth of the CycA mutant with lactate and sulfate was little affected, growth with pyruvate and sulfate was significantly impaired. We have explored the phenotype of the CycA mutant through physiological tests and transcriptomic and proteomic analyses. Data reported here show that electrons from pyruvate oxidation do not reach adenylyl sulfate reductase, the enzyme catalyzing the first redox reaction during sulfate reduction, in the absence of either CycA or the type I cytochrome c 3 :menaquinone oxidoreductase transmembrane complex, QrcABCD. In contrast to the wild type, the CycA and QrcA mutants did not grow with H 2 or formate and sulfate as the electron acceptor. Transcriptomic and proteomic analyses of the CycA mutant showed that transcripts and enzymes for the pathway from pyruvate to succinate were strongly decreased in the CycA mutant regardless of the growth mode. Neither the CycA nor the QrcA mutant grew on fumarate alone, consistent with the omics results and a redox regulation of gene expression. We conclude that TpIc 3 and the Qrc complex are D. alaskensis components essential for the transfer of electrons released in the periplasm to reach the cytoplasmic adenylyl sulfate reductase and present a model that may explain the CycA phenotype through confurcation of electrons. E nvironmental impacts of the sulfate-reducing bacteria (SRB), such as the formation of toxic sulfide and corrosion of metals, stem from SRB sulfate respiration and from vigorous metal metabolism, including both reduction and oxidation. The involvement of these bacteria in microbially influenced metal corrosion (1, 2) and their possible application for the remediation of toxic metal-contaminated environments (3, 4) have driven a systems biology investigation of their metabolism. To predict or control metabolic capabilities for beneficial environmental purposes, the bioenergetic pathways of the SRB need to be elucidated in more detail.Typically, SRB of the genus Desulfovibrio use H 2 , organic acid substrates, formate, or short-chain alcohols as electron donors for sulfate reduction, a process that occurs in the cytoplasm and is mediated by soluble enzymes. With hydrogen as the source of electrons, at an environmentally relevant partial pressure of 10 Pa (reduction potential [E=] ϭ Ϫ300 mV) (5), the first two-electron reduction of sulfate to sulfite (E 0 = ϭ Ϫ516 mV) cannot be accomplished without an additional energy input. Sulfate is activated at the expense of two ATP equivalents through the activity of sulfate adenylyltransferase (equation 1), producing adenosine phosphosulfate (APS), which increases th...

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Growth of Sulphate-reducing Bacteria by Fumarate Dismutation

Cited by 50 publications

References 5 publications

Characterization of Desulfovibrio fructosovorans sp. nov.

Characterization of Desulfovibrio fructosovorans sp. nov.

Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria

New Model for Electron Flow for Sulfate Reduction in Desulfovibrio alaskensis G20

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