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Reaction Mechanism of Molybdoenzyme Formate Dehydrogenase

Chemistry – A European Journal, 2008
AbstractFormate dehydrogenase is a molybdoenzyme of the anaerobic formate hydrogen lyase complex of the Escherichia coli microrganism that catalyzes the oxidation of formate to carbon dioxide. The two proposed mechanisms of reaction, which differ in the occurrence of a direct coordination or not of a SeCys residue to the molybdenum metal during ...
LEOPOLDINI M   +3 more
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Molybdenum and tungsten-dependent formate dehydrogenases

JBIC Journal of Biological Inorganic Chemistry, 2014
The prokaryotic formate metabolism is considerably diversified. Prokaryotes use formate in the C1 metabolism, but also evolved to exploit the low reduction potential of formate to derive energy, by coupling its oxidation to the reduction of numerous electron acceptors. To fulfil these varied physiological roles, different types of formate dehydrogenase
Luisa B, Maia   +2 more
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Engineering a Formate Dehydrogenase for NADPH Regeneration**

ChemBioChem, 2023
AbstractNicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide phosphate (NADPH) constitute major hydrogen donors for oxidative/reductive bio‐transformations. NAD(P)H regeneration systems coupled with formate dehydrogenases (FDHs) represent a dreamful method.
Wei Ma   +5 more
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Nadp+-dependent formate dehydrogenase: a review

Biocatalysis and Biotransformation, 2020
NADPH-dependent oxidoreductases are crucial biocatalysts for the industrial production of chiral compounds.
Saadet Alpdagtas, Barış Binay
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Catalytic mechanism and application of formate dehydrogenase

Biochemistry (Moscow), 2004
NAD+-dependent formate dehydrogenase (FDH) is an abundant enzyme that plays an important role in energy supply of methylotrophic microorganisms and in response to stress in plants. FDH belongs to the superfamily of D-specific 2-hydroxy acid dehydrogenases.
V I, Tishkov, V O, Popov
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[67] Formate dehydrogenase

1966
Publisher Summary This chapter discusses the determination of formate dehydrogenase. The assay depends on measurement of the rate of increase of optical density at 340 mμ consequent on the reduction of diphosphopyridine nucleotide (DPN) in the presence of formate. The complete reaction system in a 1.5 ml silica cell (1 cm light path) consists of 0.25
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Hydrogenases and formate dehydrogenases of Syntrophobacter fumaroxidans

Antonie van Leeuwenhoek, 2002
The syntrophic propionate-oxidizing bacterium Syntrophobacter fumaroxidans possesses two distinct formate dehydrogenases and at least three distinct hydrogenases. All of these reductases are either loosely membrane-associated or soluble proteins and at least one of the hydrogenases is located in the periplasm. These enzymes were expressed on all growth
de Bok, F.A.M.   +2 more
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Molybdenum-containing CO dehydrogenase and formate dehydrogenases

The molybdenum-containing CO dehydrogenase and the formate dehydrogenases catalyze important interconversions of one-carbon compounds, the former oxidizing CO to CO2, and the latter the reversible interconversion of CO2 and formate. Methodologies to study these two enzymes are discussed.
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Metabolite-modulated complex formation between .alpha.-glycerophosphate dehydrogenase and lactate dehydrogenase

Biochemistry, 1993
A modified Hummel-Dreyer equilibrium chromatography technique was used to test the hypothesis that NADH induces the molecular association of lactate dehydrogenase (LDH) and alpha-glycerol-3-phosphate dehydrogenase (alpha-GDH). In the presence of a very limited NADH concentration, a unique elution profile with a new peak running immediately ahead of a ...
H, Yong, G A, Thomas, W L, Peticolas
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Reductive activation of CO2 by formate dehydrogenases

2018
Two factors, climate change brought on by rising atmospheric CO2 levels and the accelerating shift toward renewable energy sources, have together worked to heighten interest in understanding how biological catalysts so effectively bring about the reduction of CO2 to formate, with potential applications for both bioremediation and energy storage.
Dimitri, Niks, Russ, Hille
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