Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii

Jones, J. Bryan; Dilworth, Gregory L.; Stadtman, Thressa C.

doi:10.1016/0003-9861(79)90351-5

Cited by 106 publications

(55 citation statements)

References 12 publications

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“…Both fdhA alleles contained a TGA codon at amino acid 132 (fdhA1) or 133 (fdhA2) which presumably encodes a selenocysteine residue. The presence of selenocysteine is not uncommon in formate dehydrogenases (8,10).…”

Section: Resultsmentioning

confidence: 99%

Function and Regulation of the Formate Dehydrogenase Genes of the Methanogenic ArchaeonMethanococcus maripaludis

2003

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Methanococcus maripaludis is a mesophilic species of Archaea capable of producing methane from two substrates: hydrogen plus carbon dioxide and formate. To study the latter, we identified the formate dehydrogenase genes of M. maripaludis and found that the genome contains two gene clusters important for formate utilization. Phylogenetic analysis suggested that the two formate dehydrogenase gene sets arose from duplication events within the methanococcal lineage. The first gene cluster encodes homologs of formate dehydrogenase ␣ (FdhA) and ␤ (FdhB) subunits and a putative formate transporter (FdhC) as well as a carbonic anhydrase analog. The second gene cluster encodes only FdhA and FdhB homologs. Mutants lacking either fdhA gene exhibited a partial growth defect on formate, whereas a double mutant was completely unable to grow on formate as a sole methanogenic substrate. Investigation of fdh gene expression revealed that transcription of both gene clusters is controlled by the presence of H 2 and not by the presence of formate.Hydrogen and carbon dioxide are common substrates for methanogenic Archaea. Many species of hydrogenotrophic methanogens can use formate in place of H 2 , while others cannot. The ability to use formate can be attributed to the enzyme formate dehydrogenase, which in methanogens catalyzes the reaction that produces reduced coenzyme F 420 from the oxidation of formate (9, 10, 18). The enzyme consists of two protein subunits (17), ␣ and ␤, encoded by fdhA and fdhB, respectively (15,19).The presence or absence of formate dehydrogenase genes does not predict the ability to grow on formate. Species known to contain contiguously encoded homologs of fdhA and fdhB include Methanococcus maripaludis, Methanococcus voltae, Methanobacterium formicicum, Methanococcus jannaschii, and Methanopyrus kandleri. Of these species, only the first three can use formate (4). In the species Methanothermobacter thermautotrophicus, strain Z-245 can use formate but strain ⌬H cannot. This difference is attributed to the presence in the former strain of fdh genes that are absent from the same genomic context in the latter (15). Nevertheless, fdhA and fdhB homologs are present in the genome of strain ⌬H, albeit not closely related to those known in strain Z-245. Furthermore, at least one species that is unable to grow on formate, M. jannaschii, possesses formate dehydrogenase enzyme activity (11).The organization and regulation of formate dehydrogenase genes have been studied in M. formicicum (23) and M. thermoautotrophicus strain Z-245 (15), both of which use formate. In each species a gene designated fdhC precedes fdhA and fdhB. FdhC contains several potential membrane-spanning regions (23) and may encode a formate transporter. Northern blots in both species indicated the presence of three mRNA types, one containing fdhC, fdhA, and fdhB, another containing fdhC alone, and the third containing fdhA and fdhB. An apparent transcription start site was identified upstream of fdhC in both species. The smaller mRNAs could be ...

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Section: Resultsmentioning

confidence: 99%

Function and Regulation of the Formate Dehydrogenase Genes of the Methanogenic ArchaeonMethanococcus maripaludis

2003

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“…6). Southern blot analysis indicated that a single region on the chromosome was homologous to the probe used for Northern (11,12). The molybdenum content of the medium was adjusted to limit the synthesis of active formate dehydrogenase in H2-CO2-grown M. formicicum; however, growth on H2-CO2 was not influenced.…”

Section: Resultsmentioning

confidence: 99%

Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum

1988

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“…Whereas Mb. formicicum carries a gene that encodes a single Ffd, Methanococcus vannielii carries genes that encode both selenium-free and selenium-containing variants of the Ffd (185,264). Selenium supplementation markedly stimulates formate-driven growth of the organism, suggesting that the selenocysteine-containing Ffd may be the more efficient variant (265).…”

Section: Ffd: F 420 -Reducing Formate Dehydrogenasementioning

confidence: 99%

Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions

Greening

Ahmed

Mohamed

et al. 2016

Microbiol Mol Biol Rev

159

208

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SUMMARY5-Deazaflavin cofactors enhance the metabolic flexibility of microorganisms by catalyzing a wide range of challenging enzymatic redox reactions. While structurally similar to riboflavin, 5-deazaflavins have distinctive and biologically useful electrochemical and photochemical properties as a result of the substitution of N-5 of the isoalloxazine ring for a carbon. 8-Hydroxy-5-deazaflavin (Fo) appears to be used for a single function: as a light-harvesting chromophore for DNA photolyases across the three domains of life. In contrast, its oligoglutamyl derivative F420is a taxonomically restricted but functionally versatile cofactor that facilitates many low-potential two-electron redox reactions. It serves as an essential catabolic cofactor in methanogenic, sulfate-reducing, and likely methanotrophic archaea. It also transforms a wide range of exogenous substrates and endogenous metabolites in aerobic actinobacteria, for example mycobacteria and streptomycetes. In this review, we discuss the physiological roles of F420in microorganisms and the biochemistry of the various oxidoreductases that mediate these roles. Particular focus is placed on the central roles of F420in methanogenic archaea in processes such as substrate oxidation, C1pathways, respiration, and oxygen detoxification. We also describe how two F420-dependent oxidoreductase superfamilies mediate many environmentally and medically important reactions in bacteria, including biosynthesis of tetracycline and pyrrolobenzodiazepine antibiotics by streptomycetes, activation of the prodrugs pretomanid and delamanid byMycobacterium tuberculosis, and degradation of environmental contaminants such as picrate, aflatoxin, and malachite green. The biosynthesis pathways of Foand F420are also detailed. We conclude by considering opportunities to exploit deazaflavin-dependent processes in tuberculosis treatment, methane mitigation, bioremediation, and industrial biocatalysis.

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Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii

Cited by 106 publications

References 12 publications

Function and Regulation of the Formate Dehydrogenase Genes of the Methanogenic ArchaeonMethanococcus maripaludis

Function and Regulation of the Formate Dehydrogenase Genes of the Methanogenic ArchaeonMethanococcus maripaludis

Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum

Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions

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Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii

Cited by 106 publications

References 12 publications

Function and Regulation of the Formate Dehydrogenase Genes of the Methanogenic ArchaeonMethanococcus maripaludis

Function and Regulation of the Formate Dehydrogenase Genes of the Methanogenic ArchaeonMethanococcus maripaludis

Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum

Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions

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Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions