ArticleJournal of bioenergetics and biomembranes2002
The quinol:fumarate oxidoreductase from the sulphate reducing bacterium Desulfovibrio gigas: spectroscopic and redox studies.
Article in Journal of bioenergetics and biomembranes, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 25 citations in OpenAlex.
- Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas.Scientific reports · 2018Article
- Expression of a metagenome-derived fumarate reductase from marine microorganisms and its characterization.Folia microbiologica · 2013Article
- Global transcriptome analysis of the tetrachloroethene-dechlorinating bacterium Desulfitobacterium hafniense Y51 in the presence of various electron donors and terminal electron acceptors.Journal of industrial microbiology & biotechnology · 2012Article
- The cytochrome bd respiratory oxygen reductases.Biochimica et biophysica acta · 2011Review
- A soluble NADH-dependent fumarate reductase in the reductive tricarboxylic acid cycle of Hydrogenobacter thermophilus TK-6.Journal of bacteriology · 2008Article
- Genetic characterization of a single bifunctional enzyme for fumarate reduction and succinate oxidation in Geobacter sulfurreducens and engineering of fumarate reduction in Geobacter metallireducens.Journal of bacteriology · 2006Article
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5 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The membrane bound fumarate reductase (FRD) from the sulphate-reducer Desulfovibrio gigas was purified from cells grown on a fumarate/sulphate medium and extensively characterized. The FRD is isolated with three subunits of apparent molecular masses of 71, 31, and 22 kDa. The enzyme is capable of both fumarate reduction and succinate oxidation, exhibiting a higher specificity toward fumarate (Km for fumarate is 0.42 and for succinate 2 mM) and a reduction rate 30 times faster than that for oxidation. Studies by Visible and EPR spectroscopies allowed the identification of two B-type haems and the three iron-sulplur clusters usually found in FRDs and succinate dehydrogenases: [2Fe-2S]2+/1+ (S1), [4Fe-4S]2+/1+ (S2), and [3Fe-4S]1+/0 (S3). The apparent macroscopic reduction potentials for the metal centers, at pH 7.6, were determined by redox titrations: -45 and -175 mV for the two haems, and +20 and -140 mV for the S3 and SI clusters, respectively. The reduction potentials of the haem groups are pH dependent, supporting the proposal that fumarate reduction is associated with formation of the membrane proton gradient. Furthermore, co-reconstitution in liposomes of D. gigas FRD, duroquinone, and D. gigas cytochrome bd shows that this system is capable of coupling succinate oxidation with oxygen reduction to water.
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