The need for selenite and molybdate in the formation of formic dehydrogenase by members of the <i>Coli-aerogenes</i> group of bacteria

Pinsent, Jane

doi:10.1042/bj0570010

Cited by 241 publications

(105 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Particularly surprising was the observation that formate still stimulated nitrosation by two mutants which lack all three known formate dehydrogenases ( Table 5 ) . One of these strains, JCB3882, carries three separate mutations in each of the three operons encoding the formate dehydrogenases ; the other strain, JCB3881, is pleiotropically negative due to the deletion of a gene required for the insertion of an essential selenocysteine residue in all three formate dehydrogenase molybdoproteins (Pinsent, 1954;Lester & DeMoss, 1971 ;Sawers et al, 1991). Two further tests were used to confirm that these mutants had been constructed correctly and had not reverted.…”

Section: Nitrosation Activity Of Strains Defective In Formate De Hyd mentioning

confidence: 99%

A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12

Metheringham

Cole

1997

Microbiology

View full text Add to dashboard Cite

Anaerobic, but not aerobic, cultures of Escherichia coli K-12 catalysed the rapid nitrosation of the model substrate 2,3=diaminonaphthaIene when incubated with nitrite. Formate and lactate were effective electron donors for the nitrosation reaction, which was inhibited by nitrate. Optimal growth conditions for the expression of nitrosation activity by various strains and mutants were determined. Highest activities were found with bacteria that had been grown anaerobically in a minimal medium rather than in Lennox broth, with glycerol and fumarate rather than glucose as the main carbon and energy source, and in the presence of a low concentration of nitrate. Bacteria harvested in the early exponential phase were more active than those harvested in later stages of growth. Well-characterized mutants defective in the synthesis of one or more anaerobically induced electron transfer chains were screened for nitrosation activity under these optimal growth conditions: only the respiratory nitrate reductase encoded by the narGHJ/ operon was implicated as a major contributor to nitrosation activity. Due to the limited sensitivity of the assays currently available, a minor contribution from the two alternative nitrate reductases or even other molybdoproteins could not be excluded. The role of formate in nitrosation was complex and was clearly not limited simply t o that of an electron donor in the bacterial reduction of nitrite t o nitric oxide: at least two further, chemical roles were inferred. This extensive study of more than 400 independent cultures of E. coli K-12 and its derivatives resolved some, but not all, of the apparently conflicting data in the literature concerning nitrosation catalysed by enteric bacteria.

show abstract

Section: Nitrosation Activity Of Strains Defective In Formate De Hyd mentioning

confidence: 99%

A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12

Metheringham

Cole

1997

Microbiology

View full text Add to dashboard Cite

show abstract

“…Yet in 1954 selenium was found to be required for formate dehydrogenase activity in bacteria (1) and its presence in glutathione peroxidase was demonstrated in 1973 (2). The occurrence of selenocysteine (Sec) as the selenium moiety in naturally occurring proteins was first discovered in 1976 (3).…”

Section: Introductionmentioning

confidence: 99%

How an obscure archaeal gene inspired the discovery of selenocysteine biosynthesis in humans

Hohn

Palioura

et al. 2008

IUBMB Life

View full text Add to dashboard Cite

show abstract

“…Already in 1954 selenium was rated as a growth factor of certain bacteria (Pinsent, 1954). The first bacterial selenoproteins were described in 1973 (Andreesen and Ljungdahl, 1973;Turner and Stadtman 1973), and the growing diversity of enzymatic functions of such prokaryotic enzymes remains a valuable guide to unraveling the roles of less accessible mammalian enzymes.…”

Section: Introduction: Some Historical Landmarksmentioning

confidence: 99%

Selenium in Biology: Facts and Medical Perspectives

Köhrl¹,

Brigelius‐Flohé²,

Böck³

et al. 2000

Biological Chemistry

245

143

View full text Add to dashboard Cite

Several decades after the discovery of selenium as an essential trace element in vertebrates approximately 20 eukaryotic and more than 15 prokaryotic selenoproteins containing the 21 st proteinogenic amino acid, selenocysteine, have been identified, partially characterized or cloned from several species. Many of these proteins are involved in redox reactions with selenocysteine acting as an essential component of the catalytic cycle. Enzyme activities have been assigned to the glutathione peroxidase family, to the thioredoxin reductases, which were recently identified as selenoproteins, to the iodothyronine deiodinases, which metabolize thyroid hormones, and to the selenophosphate synthetase 2, which is involved in selenoprotein biosynthesis. Prokaryotic selenoproteins catalyze redox reactions and formation of selenoethers in (stress-induced) metabolism and energy production of E. coli, of the clostridial cluster XI and of other prokaryotes. Apart from the specific and complex biosynthesis of selenocysteine, selenium also reversibly binds to proteins, is incorporated into selenomethionine in bacteria, yeast and higher plants, or posttranslationally modifies a catalytically essential cysteine residue of CO dehydrogenase. Expression of individual eukaryotic selenoproteins exhibits high tissue specificity, depends on selenium availability, in some cases is regulated by hormones, and if impaired contributes to several pathological conditions. Disturbance of selenoprotein expression or function is associated with deficiency syndromes (Keshan and Kashin-Beck disease), might contribute to tumorigenesis and atherosclerosis, is altered in several bacterial and viral infections, and leads to infertility in male rodents.

show abstract

The need for selenite and molybdate in the formation of formic dehydrogenase by members of the Coli-aerogenes group of bacteria

Cited by 241 publications

References 5 publications

A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12

A reassessment of the genetic determinants, the effect of growth conditions and the availability of an electron donor on the nitrosating activity of Escherichia coli K-12

How an obscure archaeal gene inspired the discovery of selenocysteine biosynthesis in humans

Selenium in Biology: Facts and Medical Perspectives

Contact Info

Product

Resources

About