Formate dehydrogenases from<i>Escherichia coli</i>

Giordano, Gérard; Medani, Claire-Lise; Mandrand‐Berthelot, Marie‐Andrée; Boxer, David H.

doi:10.1111/j.1574-6968.1983.tb00396.x

Cited by 26 publications

(1 citation statement)

References 18 publications

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“…The fermentative production of gas from glucose by members of the family Enterobacteriaceae results from the activity of the formate hydrogenlyase system which consists of formate dehydrogenase (FDH), hydrogenase, and one or two as yet unidentified intermediates (8,20,21). This hydrogenase-linked FDH (FDHH) has been shown to be distinct from the nitrate reductase-linked FDH (FDHN) both in structure (9,12) and in the ability to donate electrons to certain artificial electron acceptors; FDHH will reduce benzyl viologen but not methylene blue or phenazine methosulfate, whereas FDHN has the opposite specificity (19). However, the two enzymes also share important features, as both are selenoenzymes (15,21), and mutants which lack both activities, i.e., fdh mutants, are more frequently isolated than mutants which lack specifically one or the other, i.e., fhl or fdn mutants (3,4,8,17).…”

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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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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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Formate Dehydrogenase: Microbiology, Biochemistry and Genetics

Ferry

1990

Autotrophic Microbiology and One-Carbon Metabolism

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Interspecies compatibility of selenoprotein biosynthesis in Enterobacteriaceae

Heider¹,

Forchhammer²,

Sawers³

et al. 1991

Arch. Microbiol.

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Several species of Enterobacteriaceae were investigated for their ability to synthesize selenium-containing macromolecules. Seleniated tRNA species as well as seleniated polypeptides were formed by all organisms tested. Two selenopolypeptides could be identified in most of the organisms which correspond to the 80 kDa and 110 kDa subunits of the anaerobically induced formate dehydrogenase isoenzymes of E. coli. In those organisms possessing both isoenzymes, their synthesis was induced in a mutually exclusive manner dependent upon whether nitrate was present during anaerobic growth. The similarity of the 80 kDa selenopolypeptide among the different species was assessed by immunological and genetic analyses. Antibodies raised against the 80 kDa selenopolypeptide from E. coli cross-reacted with an 80 kDa polypeptide in those organisms which exhibited fermentative formate dehydrogenase activity. These organisms also contained genes which hybridised with the fdhF gene from E. coli. In an attempt to identify the signals responsible for incorporation of selenium into the selenopolypeptides in these organisms we cloned a portion of the fdhF gene homologue from Enterobacter aerogenes. The nucleotide sequence of the cloned 723 bp fragment was determined and it was shown to contain an in-frame TGA (stop) codon at the position corresponding to that present in the E. coli gene. This fragment was able to direct incorporation of selenocysteine when expressed in the heterologous host, E. coli. Moreover, the E. coli fdhF gene was expressed in Salmonella typhimurium, Serratia marcescens and Proteus mirabilis, indicating a high degree of conservation of the seleniating system throughout the enterobacteria.

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Formate dehydrogenases fromEscherichia coli

Cited by 26 publications

References 18 publications

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

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

Formate Dehydrogenase: Microbiology, Biochemistry and Genetics

Interspecies compatibility of selenoprotein biosynthesis in Enterobacteriaceae

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