The Oxidation of Methylamine in <i>Paracoccus denitrificans</i>

Gier, J.-W. L. De; Oost, John van der; Harms, N.; Stouthamer, A. H.; Spanning, Rob J.M. van

doi:10.1111/j.1432-1033.1995.0148l.x

Cited by 16 publications

(6 citation statements)

References 47 publications

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“…Yields on methanol were relatively low compared to those seen with methylamine for both strains S1 and TGA (Table 3). As methanol and methylamine are both dehydrogenated to give formaldehyde (De Gier et al 1995), similar yields would be expected, as observed with other methylotrophs (Goldberg et al 1976;Van Verseveld and Stouthamer 1978;Suylen et al 1986;Wood et al 1998). The less efficient use of methanol cannot yet be explained.…”

Section: Discussionsupporting

confidence: 60%

Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter

et al. 2000

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Dimethylsulfone is a major product of the chemical oxidation in the atmosphere of the principal biogenic sulfur gas, dimethylsulfide, but no studies have been reported on the mechanisms for its microbiological degradation. Three novel strains of bacteria have been isolated from enrichment cultures provided with dimethylsulfone as the only carbon and energy substrate. These are novel facultatively methylotrophic species of Hyphonmicrobium and Arthobacter, capable of growth on a range of one-carbon substrates. Cell-free extracts contained activities of enzymes necessary for a reductive/oxidative pathway for dimethylsulfone degradation: membrane-bound-dimethylsulfone and dimethylsulfoxide reductases, dimethylsulfide monooxygenase, and methanethiol oxidase. Enzymatic evidence is also presented for the subsequent oxidation of formaldehyde by formaldehyde and formate dehydrogenases in the Hyphomicrobium strain and by a dissimilatory ribulose monophosphate cycle in the Arthrobacter strains. The strains also grew on dimethylsulfoxide and dimethylsulfide, and dimethylsulfide-grown bacteria oxidized dimethylsulfide and dimethylsulfoxide but not dimethylsulfone. Formaldehyde assimilation was effected in the Hyphomicrobium strain by the serine pathway, but enzymes of the ribulose monophosphate cycle for formaldehyde assimilation were present in the Arthrobacter strains grown on dimethylsulfone. In contrast, one of the Arthrobacter strains was shown to switch to the serine pathway during growth on methanol. Growth yields on dimethylsulfone and formaldehyde were consistent with the occurrence of the serine pathway in Hyphomicrobium strain S1 and the ribulose monophosphate cycle in Arthrobacter strain TGA, and with the proposed reductive pathway for dimethylsulfone degradation in both.

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Section: Discussionsupporting

confidence: 60%

Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter

et al. 2000

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“…From pUCpcco a 965‐bp Kpn I– Pst I fragment was cloned into pBK11SL ( Kpn I– Pst I), yielding plasmid pPr271. A 637‐bp Eco RI– Eco RV fragment from pUCc5501, which contained the cta DII promoter [28], was cloned into pBK11 ( Eco RI– Sma I). This pBK11 derivative was named pPr231.…”

Section: Methodsmentioning

confidence: 99%

“…The forward primer contained the nucleotides from positions 79 through 97 of the sequence of the qox locus of P. denitrificans [7] (5 H -CGCCGCAATTGCCACGTTCTCATAGCTGGG), adapted to contain a MunI restriction site (underlined). The reversed one contained the complementary bases from position 710 through 728 (5 H -CCGGCGGATCCGGAAT-CAGCAAGGCAAGCC), adapted with a BamHI restriction pUC19 der., cycA, ctaDII [28] site (underlined). The PCR product was checked by sequence analysis (dna strider 1.0 and geneworks 2.3) and then cloned in pBK11.…”

Section: Dna Manipulations and Mutagenesismentioning

confidence: 99%

Regulation of expression of terminal oxidases in Paracoccus denitrificans

Otten

Stork

Reijnders

et al. 2001

European Journal of Biochemistry

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In order to study the induction of terminal oxidases in Paracoccus denitrificans, their promoters were fused to the lacZ reporter gene and analysed in the wild-type strain, in an FnrP-negative mutant, in a cytochrome bc 1 -negative mutant, and in six single or double oxidase-negative mutant strains. The strains were grown under aerobic, semi-aerobic, and denitrifying conditions. The oxygen-sensing transcriptional-regulatory protein FnrP negatively regulated the activity of the qox promoter, which controls expression of the ba 3 -type quinol oxidase, while it positively regulated the activity of the cco promoter, which controls expression of the cbb 3 -type cytochrome c oxidase. The ctaDII and ctaC promoters, which control the expression of the aa 3 -type cytochrome c oxidase subunits I and II, respectively, were not regulated by FnrP. The activities of the latter two promoters, however, did decrease with decreasing oxygen concentrations in the growth medium, suggesting that an additional oxygen-sensing mechanism exists that regulates transcription of ctaDII and ctaC. Apparently, the intracellular oxygen concentration (as sensed by FnrP) was not the only signal to which the oxidase promoters responded. At given extracellular oxygen status, both the qox and the cco promoters responded to mutations in terminal oxidase genes, whereas the ctaDII and ctaC promoters did not. The change of electron distribution through the respiratory network, resulting from elimination of one or more oxidase genes, may have changed intracellular signals that affect the activities of the qox and cco promoters. On the other hand, the re-routing of electron distribution in the respiratory mutants hardly affected the oxygen consumption rate as compared to that of the wildtype. This suggests that the mutants adapted their respiratory network in such a way that they were able to consume oxygen at a rate similar to that of the wild-type strain.

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“…41 However, the electron-transfer kinetics study 42 and the X-ray structure analysis 43 of MADH complexed with amicyanin and cytochrome c 551 demonstrated that amicyanine shows high specificity for MADH in P. denitrificans. However, Methylomonas sp.…”

Section: Comparison Of the Structures Between Az-iso2 And Amicyaninmentioning

confidence: 97%

The Significance of the Flexible Loop in the Azurin (Az-iso2) from the Obligate Methylotroph Methylomonas sp. Strain J

Inoue

Suzuki

Nishio

et al. 2003

Journal of Molecular Biology

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The Oxidation of Methylamine in Paracoccus denitrificans

Cited by 16 publications

References 47 publications

Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter

Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter

Regulation of expression of terminal oxidases in Paracoccus denitrificans

The Significance of the Flexible Loop in the Azurin (Az-iso2) from the Obligate Methylotroph Methylomonas sp. Strain J

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