The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli.

Enoch, Harry G.; Lester, Robert L.

doi:10.1016/s0021-9258(19)40989-7

Cited by 312 publications

(37 citation statements)

References 78 publications

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“…Formate dehydrogenase activities were monitored spectrophotometrically by following the reduction of artificial electron acceptors. The reduction of BV was followed at 600 nm (5). The reduction of phenazine methosulfate was followed by coupling the reduction to dichlorophenolindophenol (19).…”

Section: Methodsmentioning

confidence: 99%

“…It has been established that the formate dehydrogenase activities present under these two sets of conditions have differing electron acceptor specificities. The formate dehydrogenase formed in the absence of nitrate transfers electrons to benzyl viologen (BV) preferentially (12,15), whereas that formed in the presence of nitrate preferentially uses methylene blue or phenazine methosulfate (PMS) as an electron acceptor (5,12,17).…”

mentioning

confidence: 99%

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Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli

Cox¹,

Edwards²,

DeMoss³

1981

J Bacteriol

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Formate dehydrogenase, a component activity of two alternative electron transport pathways in anaerobic Escherichia coli, has been resolved as two distinguishable enzymes. One, which was induced with nitrate reductase as a component of the formate-nitrate reductase pathway, utilized phenazine methosulfate (PMS) in preference to benzyl viologen (BV) as an artificial electron acceptor and appeared to be exclusively membrane-bound. A second formate dehydrogenase, which was induced as a component of the formate hydrogenlyase pathway, appeared to exist both as a membrane-bound form and as a cytoplasmic enzyme; the cytoplasmic activity was resolved completely from the PMS-linked activity on a sucrose gradient. When E. coli was grown in the presence of 75Se-selenite, a 110,000-dalton selenopeptide, previously shown to be a component of the PMS-linked enzyme, was induced and repressed with this activity. In contrast, an 80,000-dalton selenopeptide was induced and repressed with the BV-linked activity and exhibited a distribution similar to the BV-linked formate dehydrogenase in cell fractions and in sucrose gradients. The results indicate that the two formate dehydrogenases are distinguishable on the basis of their artificial electron acceptor specificity, their cellular localization, and the size of their respective selenoprotein components.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli

Cox¹,

Edwards²,

DeMoss³

1981

J Bacteriol

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“…Such arrangement resulting in short diffusion distances for quinone molecules may increase the electron transfer efficiency from FdnGHI to NarGHI as proposed in the solid-state model. Finally, the reported co-purification of FdnGHI and NarGHI complexes over a wide-range of conditions (Enoch and Lester, 1975;Jormakka et al, 2002a) may be suggestive of their physical association. Furthermore, Claypool et al (Claypool et al, 2008;Claypool, 2009) reported that CL defines the functional interactome of the mitochondrial ADP/ATP carrier known to associate with the respiratory supercomplexes.…”

Section: Lipidsmentioning

confidence: 85%

Supramolecular Organization in Prokaryotic Respiratory Systems

Magalon

Arias-Cartin

Walburger

2012

Advances in Microbial Physiology

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Prokaryotes are characterized by an extreme flexibility of their respiratory systems allowing them to cope with various extreme environments. To date, supramolecular organization of respiratory systems appears as a conserved evolutionary feature as supercomplexes have been isolated in bacteria, archaea, and eukaryotes. Most of the yet identified supercomplexes in prokaryotes are involved in aerobic respiration and share similarities with those reported in mitochondria. Supercomplexes likely reflect a snapshot of the cellular respiration in a given cell population. While the exact nature of the determinants for supramolecular organization in prokaryotes is not understood, lipids, proteins, and subcellular localization can be seen as key players. Owing to the well-reported supramolecular organization of the mitochondrial respiratory chain in eukaryotes, several hypotheses have been formulated to explain the consequences of such arrangement and can be tested in the context of prokaryotes. Considering the inherent metabolic flexibility of a number of prokaryotes, cellular distribution and composition of the supramolecular assemblies should be studied in regards to environmental signals. This would pave the way to new concepts in cellular respiration.

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“…The relatively high activities found in the presence of nitrate and formate are in apparent cdntradiction to the fact that nitrate in the growth medium completely represses gas production, even when formate is present (E. L. Barrett, unpublished data). However, nitrate also induces FDHN activity (3,8,11,21), and it may be that expression of FDHN interfers with gas production as is discussed below.…”

Section: Discussionmentioning

confidence: 99%

Anaerobiosis, formate, nitrate, and pyrA are involved in the regulation of formate hydrogenlyase in Salmonella typhimurium

Barrett¹,

Kwan²,

Macy³

1984

J Bacteriol

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Three groups of mutants defective in the fermentative production of gas were isolated from Salmonella typhimurium LT2 subjected to transposition mutagenesis with Mu d(Apr lac). One group consisted of strains which lacked hydrogenase. The mutation site for this group was located in the vicinity of the known hyd gene. A second group consisted of mutants which lacked the formate dehyrogenase associated with hydrogenase. The mutation site was located in four of them. It was not in the vicinity of the previously described fhlD gene but was instead located at 93 min on the Salmonella map. The third mutant group, which consisted of strains that produced gas in triple sugar iron agar but not in nutrient agar supplemented with glucose, appeared to be pyrA mutants. The insertion site was located in the vicinity of pyrA , and they required arginine and pyrimidines for growth. Expression of the lac operon in the hyd mutants was induced by anaerobiosis. It was only slightly increased by the addition of formate under anaerobic conditions and slightly decreased by the addition of nitrate. Nitrate had no effect in an hyd ::Mu d strain that also carried a chlC::Tn10 insertion. Full expression of the lac operon in the fhl mutants required both formate and anaerobic conditions. The presence of nitrate in addition to formate resulted in activities about half those obtained in its absence, even in the fhl ::Mu d chlC::Tn10 double mutant. In the absence of formate, nitrate reduced expression only in the fhl ::Mu d single mutants. Expression of the lac operon among the pyrA mutants was repressed by arginine and cytosine and also by anaerobiosis. An explanation for the involvement of pyrA in aerobic and anaerobic energy metabolism is proposed.

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The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli.

Cited by 312 publications

References 78 publications

Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli

Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli

Supramolecular Organization in Prokaryotic Respiratory Systems

Anaerobiosis, formate, nitrate, and pyrA are involved in the regulation of formate hydrogenlyase in Salmonella typhimurium

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