Formate Dehydrogenase: Microbiology, Biochemistry and Genetics

Ferry, James G.

doi:10.1007/978-94-009-1978-5_5

Cited by 10 publications

(4 citation statements)

References 132 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enrichment of FDH coincided with detection of a 42-kDa protein (Fig. 2, lane 4), which parallels the subunit size reported for cytosolic FDHs from a number of organisms (7). As far as we are aware, this is the only time that induction of FDH by cyanide has been reported in any organism.…”

Section: Vol 70 2004 Pterin-dependent Cyanide Oxidation In P Fluorsupporting

confidence: 85%

Enzymatic Assimilation of Cyanide via Pterin-Dependent Oxygenolytic Cleavage to Ammonia and Formate in Pseudomonas fluorescens NCIMB 11764

Fernandez

Dolghih

Kunz

2004

Appl Environ Microbiol

View full text Add to dashboard Cite

Utilization of cyanide as a nitrogen source by Pseudomonas fluorescens NCIMB 11764 occurs via oxidative conversion to carbon dioxide and ammonia, with the latter compound satisfying the nitrogen requirement. Substrate attack is initiated by cyanide oxygenase (CNO), which has been shown previously to have properties of a pterin-dependent hydroxylase. CNO was purified 71-fold and catalyzed the quantitative conversion of cyanide supplied at micromolar concentrations (10 to 50 M) to formate and ammonia. The specific activity of the partially purified enzyme was approximately 500 mU/mg of protein. The pterin requirement for activity could be satisfied by supplying either the fully (tetrahydro) or partially (dihydro) reduced forms of various pterin compounds at catalytic concentrations (0.5 M). These compounds included, for example, biopterin, monapterin, and neopterin, all of which were also identified in cell extracts. Substrate conversion was accompanied by the consumption of 1 and 2 molar equivalents of molecular oxygen and NADH, respectively. When coupled with formate dehydrogenase, the complete enzymatic system for cyanide oxidation to carbon dioxide and ammonia was reconstituted and displayed an overall reaction stoichiometry of 1:1:1 for cyanide, O 2 , and NADH consumed. Cyanide was also attacked by CNO at a higher concentration (1 mM), but in this case formamide accumulated as the major reaction product (formamide/formate ratio, 0.6:0.3) and was not further degraded. A complex reaction mechanism involving the production of isocyanate as a potential CNO monooxygenation product is proposed. Subsequent reduction of isocyanate to formamide, whose hydrolysis occurs as a CNO-bound intermediate, is further envisioned. To our knowledge, this is the first report of enzymatic conversion of cyanide to formate and ammonia by a pterin-dependent oxygenative mechanism.

show abstract

Section: Vol 70 2004 Pterin-dependent Cyanide Oxidation In P Fluorsupporting

confidence: 85%

Enzymatic Assimilation of Cyanide via Pterin-Dependent Oxygenolytic Cleavage to Ammonia and Formate in Pseudomonas fluorescens NCIMB 11764

Fernandez

Dolghih

Kunz

2004

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Several additional selenium compounds (sodium selenate, selenium dioxide and selenocystine) added at 50 nM concentrations similarly did not influence growth rate. As molybdenum is an essential cofactor in FDH enzymes (Ferry, 1990a), we tested whether or not Mo was growth limiting at the concentration routinely used to grow T. primitia (36 µg l −1 ). Higher sodium molybdate concentrations (360 µg l −1 , 1.8 mg l −1 or 18 mg l −1 ) provided no growth benefit.…”

Section: Resultsmentioning

confidence: 99%

Selenium controls transcription of paralogous formate dehydrogenase genes in the termite gut acetogen, Treponema primitia

Matson

Zhang

Leadbetter

2010

Environmental Microbiology

View full text Add to dashboard Cite

SummaryThe termite gut spirochete, Treponema primitia, is a CO 2-reductive acetogen that is phylogenetically distinct from other distantly related and more extensively studied acetogens such as Moorella thermoacetica. Research on T. primitia has revealed details about the role of spirochetes in CO 2-reductive acetogenesis, a process important to the mutualism occurring between termites and their gut microbial communities. Here, a locus of the T. primitia genome containing Wood-Ljungdahl pathway genes for CO 2-reductive acetogenesis was sequenced. This locus contained methyl-branch genes of the pathway (i.e. for the reduction of CO 2 to the level of methyltetrahydrofolate) including paralogous genes for cysteine and selenocysteine (Sec) variants of formate dehydrogenase (FDH) and genes for Sec incorporation. The FDH variants affiliated phylogenetically with hydrogenase-linked FDH enzymes, suggesting that T. primitia FDH enzymes utilize electrons derived directly from molecular H 2. Sub-nanomolar concentrations of selenium decreased transcript levels of the cysteine variant FDH gene. Selenium concentration did not markedly influence the level of mRNA upstream of the Sec-codon in the Sec variant FDH; however, the level of transcript extending downstream of the Sec-codon increased incrementally with increasing selenium concentrations. The features and regulation of these FDH genes are an indication that T. primitia may experience dynamic selenium availability in its H 2-rich gut environment.

show abstract

“…Immunostaining of soluble or total cell protein from A. eutrophus with the polyclonal anti-S-FDH-IgG revealed that S-FDH and the membrane-bound FDH do not Brought to you by | The University of Auckland Library Authenticated Download Date | 6/17/15 12:57 AM contain related epitopes recognized by the antibodies. In E. co//, the cytoplasmic FDH H was also shown to be immunologically distinct from the membrane-bound FDH N (Ferry, 1990), whereas FDH N and another membranebound enzyme, FDH 0 , share immunological similarities (Pommierefa/., 1992).…”

Section: Discussionmentioning

confidence: 95%

Structural and Immunological Studies on the Soluble Formate Dehydrogenase fromAlcaligenes eutrophus

Friedebold¹,

Mayer²,

Bill³

et al. 1995

Biological Chemistry Hoppe-Seyler

View full text Add to dashboard Cite

During growth with formate as the sole energy source the autotrophic bacterium Alcaligenes eutrophus synthesizes a cytoplasmic formate dehydrogenase. The enzyme is a molybdo-iron-sulfur-flavo protein and the major NADH-producing system under these growth conditions, although it was estimated to constitute only 0.65% of the soluble cell protein. An electron microscopic analysis of the purified enzyme revealed that the particle is made up of four nonidentical submasses, corroborating previous structural data. The NH2-terminal amino acid sequences of the enzyme subunits exhibited significant similarities to those of only one other heteromeric formate dehydrogenase, the enzyme from the methane-utilizing bacterium Methylosinus trichosporium. Metal analyses yielded 21.5 g-atom iron, 2.18 g-atom nickel, 0.76 g-atom molybdenum, and 0.59 g-atom zinc per mol of enzyme. Initial electron paramagnetic resonance spectroscopic studies showed at least three distinct signals which appeared upon reduction of the enzyme with NADH or formate. The corresponding spin systems could be attributed to iron-sulfur centers of the enzyme. Comparative immunostaining and activity-staining experiments using cell extracts from various bacteria established immunological similarities between the soluble formate dehydrogenase of A. eutrophus and the soluble enzymes from all tested facultative autotrophs as well as from M. trichosporium.

show abstract

Formate Dehydrogenase: Microbiology, Biochemistry and Genetics

Cited by 10 publications

References 132 publications

Enzymatic Assimilation of Cyanide via Pterin-Dependent Oxygenolytic Cleavage to Ammonia and Formate in Pseudomonas fluorescens NCIMB 11764

Enzymatic Assimilation of Cyanide via Pterin-Dependent Oxygenolytic Cleavage to Ammonia and Formate in Pseudomonas fluorescens NCIMB 11764

Selenium controls transcription of paralogous formate dehydrogenase genes in the termite gut acetogen, Treponema primitia

Structural and Immunological Studies on the Soluble Formate Dehydrogenase fromAlcaligenes eutrophus

Contact Info

Product

Resources

About