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Groundwater metagenome

ABSTRACT: Chloroethenes-dechlorinating consortium using gluconate as a hydrogen donor

PROVIDER: PRJDB9757 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	DRR225125_1.fastq.gz	Fastqsanger.gz
	DRR225125_2.fastq.gz	Fastqsanger.gz
	DRR225126_1.fastq.gz	Fastqsanger.gz
	DRR225126_2.fastq.gz	Fastqsanger.gz

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Project description:Four stable and robust TCE-dechlorinating microbial communities were enriched from TCE-contaminated groundwater under four different conditions exploring two parameters, high and low methanogenic activity (Meth and NoMeth), with and without vitamin B12 supplement (MethB12 and NoMethB12, Meth and NoMeth, respectively). Identical amounts of lactate (2.7 mmol) and TCE (20 μl) were supplied as electron donor and electron acceptor. All four cultures were capable of reductively dechlorinating TCE to VC and ethene. Genomic DNA of the four enrichments was applied on a quad-Dhc-genome microarray in order to characterize the gene content of Dehalococcoides species present in the four enrichments

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Characterization of four TCE-dechlorinating microbial enrichments grown with different cobalamin stress and methanogenic conditions

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Project description:Evaluation of temperature dependence on sequential chlorinated ethenes dechlorination and the dynamics of dechlorinating microorganisms

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Chance1952_Catalase_Mechanism

Project description:This model is described in the article: The mechanism of catalase action. II. Electric analog computer studies. Britton Chance, David S Greenstein, Joseph Higgins, CC Yang, Arch Biochem. 1952 37:322-39. PubmedID:14953444 Summary: An electric analog computer has been constructed for a study of the kinetics of catalase action. This computer gives results for the formation and disappearance of the catalase-hydrogen peroxide complex that are in good agreement with the experimental data. The computer study verifies an approximate method for the computation of the velocity constant for the combination of hydrogen peroxide and catalase and justifies the simple formula used previously to compute the velocity constant for the reaction of the catalase-hydrogen peroxide complex with donor molecules. Finally, the computer data show that the binding of peroxide to catalase is a practically irreversible reaction. The reaction of the enzyme-substrate complex, p, with the electron donor, a, is bimolecular, although in the article, as a is assumed to be constant, it is modelled using an apparent rate constant consisting of the product of the rate constant, k4, and the concentration of a. In this implementation, the concentration of a is set to 1 and the value of k4 just adapted so that the product equals the values given for k4*a in the article. The specific parameter values are taken from Fig 3. The graphs do not exactly match those in the paper, this may be due to the different simulators used.

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Project description:Groundwater dechlorinating microbial communities from synthetic mineral medium in Toronto, Ontario, Canada - Site contaminated with chlorinated ethenes metagenome

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