Bacterial fumarate respiration

Kröger, Achim; Geisler, Viktor; Lemma, E.; Theis, F.; Lenger, Ruth

doi:10.1007/bf00245358

Cited by 146 publications

(96 citation statements)

References 34 publications

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“…Escherichia coli possesses two class I fumarase genes, namely jiimA [3] andfumB [4] and one class II gene, fumC [5]. The gene products of jiiA and fumB are thought to function respectively under aerobic conditions in the citric acid cycle VumA) and in the generation of fumarate for use as an anaerobic electron acceptor VumB) as supported both by their differential gene regulation and by their relative affinities for fumarate and malate (reviewed in [6]). In spite of these functional differences, the class I enzymes display strong sequence similarity and immunological relatedness [ 11.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase

et al. 1994

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Fumarase catalyzes the interconversion of L-malate and fumarate. A Sulfolobus soljktaricus fumarase gene (jiimc) was cloned and sequenced. Typical archaebacterial regulatory sites were identified in the region flanking the fiC open reading frame. The fmC gene encodes a protein of 438 amino acids (47,899 Da) which shows several significant similarities with class II fumarases from both eubacterial and eukariotic sources as well as with aspartases. S. solfataricus fiunarase expressed in Escherichia coli retains enzymatic activity and its thermostability is comparable to that of .S. solfataricus purified enzyme despite a 11 amino acid C-terminal deletion.

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Section: Introductionmentioning

confidence: 99%

Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase

et al. 1994

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“…Increased fumarate reductase activity in CTAB-permeabilized cell sus-318 Table 4 Reduction of cytochrome(s) in cell extracts of G. sulfurreducens by citric acid cycle intermediates and reduced pyridine nucleotides (concentration in assays 5 and 0.5 mM, respectively). Protein content in 1 ml assay was 2.6 mg (Kröger et al 1992;Unden and Bongaerts 1997). In the iron-reducing bacterium Shewanella putrefaciens, fumarate reductase has been described as a soluble, periplasmic flavocytochrome c enzyme (Pealing et al 1992).…”

Section: Discussionmentioning

confidence: 99%

Oxidation of acetate through reactions of the citric acid cycle by Geobacter sulfurreducens in pure culture and in syntrophic coculture

Galushko

Schink

2000

Archives of Microbiology

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160

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Geobacter sulfurreducens strain PCA oxidized acetate to CO 2 via citric acid cycle reactions during growth with acetate plus fumarate in pure culture, and with acetate plus nitrate in coculture with Wolinella succinogenes. Acetate was activated by succinyl-CoA:acetate CoA-transferase and also via acetate kinase plus phosphotransacetylase. Citrate was formed by citrate synthase. Soluble isocitrate and malate dehydrogenases reduced NADP + and NAD + , respectively. Oxidation of 2-oxoglutarate was measured as benzyl viologen reduction and was strictly CoA-dependent; a low activity was also observed with NADP + . Succinate dehydrogenase and fumarate reductase both were membrane-bound. Succinate oxidation was coupled to NADP + reduction whereas fumarate reduction was coupled to NADPH and NADH oxidation. Coupling of succinate oxidation to NADP + or cytochrome(s) reduction required an ATP-dependent reversed electron transport. Net ATP synthesis proceeded exclusively through electron transport phosphorylation. During fumarate reduction, both NADPH and NADH delivered reducing equivalents into the electron transport chain, which contained a menaquinone. Overall, acetate oxidation with fumarate proceeded through an open loop of citric acid cycle reactions, excluding succinate dehydrogenase, with fumarate reductase as the key reaction for electron delivery, whereas acetate oxidation in the syntrophic coculture required the complete citric acid cycle.

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“…Acetobacterium woodii is able to reduce the acrylic side chain of caffeate (3,4-dihydroxyphenylacrylate) with H 2 and to couple this process to the synthesis of ATP (Tschech and Pfennig 1984;Hansen et al 1988). The most common and best understood type of anaerobic respiration with an unsaturated organic compound is the reduction of fumarate (Kröger et al 1992). Organisms such as Wolinella succinogenes, Escherichia coli, and Desulfovibrio gigas are able to grow by the reduction of fumarate.…”

Section: Discussionmentioning

confidence: 99%

“…Organisms such as Wolinella succinogenes, Escherichia coli, and Desulfovibrio gigas are able to grow by the reduction of fumarate. The fumarate reductase is localized at the cytoplasmic side of the cell membrane and converts fumarate to succinate without energy-rich intermediates (Kröger et al 1992). It would be interesting to know whether the mechanism of acrylate reduction in strain W218 is similar to the mechanism of fumarate reduction or to the propionate-forming pathway in bacteria with a non-randomiz- Phylogenetic relationship of Desulfovibrio acrylicus W218 with other sulfate-reducing bacteria.…”

Section: Discussionmentioning

confidence: 99%

Cleavage of dimethylsulfoniopropionate and reduction of acrylate by Desulfovibrio acrylicus sp. nov.

Maarel

vanBergeijk

Werkhoven

et al. 1996

Archives of Microbiology

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UvA-DARE is a service provided by the library of the University of Amsterdam (http://dare.uva.nl) General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). UvA-DARE (Digital AcademicRepository Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 13 May 2018Abstract From anoxic intertidal sediment, a dimethylsulfoniopropionate (DMSP)-cleaving anaerobe (strain W218) was isolated that reduced the acrylate formed to propionate. The bacterium was vibrio-to rod-shaped and motile by means of multiple polar flagella. It reduced sulfate, thiosulfate, and acrylate, and used lactate, fumarate, succinate, malate, pyruvate, ethanol, propanol, glycerol, glycine, serine, alanine, cysteine, hydrogen, and formate as electron donors. Sulfate and acrylate were reduced simultaneously; growth with sulfate was faster than with acrylate. Extracts of cells grown in the presence of DMSP contained high DMSP lyase activities (9.8 U/mg protein). The DNA mol% G+C was 45.1. On the basis of its characteristics and the 16S rRNA gene sequence, strain W218 was assigned to a new Desulfovibrio species for which the name Desulfovibrio acrylicus is proposed. A variety of other sulfate-reducing bacteria (eight of them originating from a marine or saline environment and five from other environments) did not reduce acrylate.

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Bacterial fumarate respiration

Cited by 146 publications

References 34 publications

Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase

Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase

Oxidation of acetate through reactions of the citric acid cycle by Geobacter sulfurreducens in pure culture and in syntrophic coculture

Cleavage of dimethylsulfoniopropionate and reduction of acrylate by Desulfovibrio acrylicus sp. nov.

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