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EC Number
General Information
Commentary
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enzyme structure-function relationship, overview
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the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
physiological function
a subunit MfrA mutant strain is less susceptible to H2O2 as the wildtype. The H2O2 concentration in the mutant cultures is significantly higher than that of wild-type. In the presence of H2O2, catalase activity and expression are lower in the mutant strain as compared to the wild-type. Exposure to H2O2 results in a significant decrease in total intracellular iron in the mutant strain, while the addition of iron to the growth medium mitigates H2O2 susceptibility and accumulation in the mutant. The mutant strain is significantly more persistent in RAW macrophages
physiological function
enzyme belongs to a system of electron transport phosphorylation in which formate functions as the donor and fumarate as the terminal acceptor. Menaquinone is an obligatory redox mediator of formate-fumarate reductase electron transport phosphorylation system
physiological function
fumarate reductase, which is proficient in succinate oxidation, is able to functionally replace succinate-ubiquinone oxidoreductase in aerobic respiration when conditions are used to allow the expression of the frdABCD operon aerobically. Expression of plasmids which utilize the FRD promoter of the frdABCD operon fused to the sdhCDAB genes to drive expression shows that, under anaerobic growth conditions where fumarate is utilized as the terminal electron acceptor, succinate-ubiquinone oxidoreductase would function to support anaerobic growth of Escherichia coli
physiological function
fumarate reduction by NADH is catalyzed by an electron transport chain consisting of NADH dehydrogenase NADH:menaquinone reductase, menaquinone, and succinate dehydrogenase operating in the reverse direction, i.e. menaquinol:fumarate reductase. In sdh or aro mutant strains, which lack succinate dehydrogenase or menaquinone, respectively, the activity of fumarate reduction by NADH is missing. The membrane fraction of a mutant lacking functional sdh genes catalyzes fumarate reduction by NADH or 2,3-dimethyl-1,4-naphthoquinol with less than 7% of the wild-type activities. In resting cells fumarate reduction requires glycerol or glucose as the electron donor, which presumably supply NADH for fumarate reduction
physiological function
is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate
physiological function
the enzyme is involved in anaerobic metabolism
physiological function
the enzyme is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate
physiological function
the enzyme is part of the complex II, which in the anaerobic respiratory chain of the parasitic nematode Ascaris suum, couples the reduction of fumarate to the oxidation of rhodoquinol. Critical role of the low redox potential of rhodoquinol in the fumarate reduction of Ascaris suum complex II
Results 1 - 10 of 12 > >>