The Transcriptional Regulator AlgR Controls Cyanide Production in Pseudomonas aeruginosa
- A. Carterson, L. Morici, M. Schurr
- Biology, EngineeringJournal of Bacteriology
- 15 October 2004
The data indicate that mucoid P. aeruginosa regardless of their origin (laboratory or clinically derived) produce more cyanide than their nonmucoid counterparts, AlgR regulates HCN production in P.aerug inosa, and P. Aeruginosas CF isolates are more hypercyanogenic than nonmuCOid laboratory strains.
Degradation of the metal-cyano complex tetracyanonickelate(II) by cyanide-utilizing bacterial isolates
- J. Silva-Avalos, M. Richmond, O. Nagappan, D. Kunz
- BiologyApplied and Environmental Microbiology
- 1 December 1990
Ten bacterial isolates capable of growth on tetracyanonickelate(II) [K2[Ni(CN)4]] (TCN) as the sole nitrogen source were isolated from soil, freshwater, and sewage sludge enrichments and degradation appears to parallel the capacity for growth on KCN, degradation does not occur in the presence of ammonia, and proceeds via the formation of Ni(CN),2 as a biological metabolite.
Enzymatic Assimilation of Cyanide via Pterin-Dependent Oxygenolytic Cleavage to Ammonia and Formate in Pseudomonas fluorescens NCIMB 11764
- R. Fernández, E. Dolghih, D. Kunz
- Biology, ChemistryApplied and Environmental Microbiology
- 1 January 2004
To the authors' knowledge, this is the first report of enzymatic conversion of cyanide to formate and ammonia by a pterin-dependent oxygenative mechanism.
Utilization of cyanide as nitrogenous substrate by Pseudomonas fluorescens NCIMB 11764: evidence for multiple pathways of metabolic conversion
- D. Kunz, O. Nagappan, J. Silva-Avalos, G. Delong
- BiologyApplied and Environmental Microbiology
- 1 June 1992
The growth of Pseudomonas fluorescens NCIMB 11764 on cyanide as the sole nitrogen source was accomplished by use of a modified fed-batch cultivation procedure and the relative yields of all four metabolites (CO2, formamide, formate, and ammonia) were shown to be dependent on the KCN concentration and availability of oxygen.
Accumulation of α-Keto Acids as Essential Components in Cyanide Assimilation by Pseudomonas fluorescens NCIMB 11764
- D. Kunz, Jui-Lin Chen, G. Pan
- BiologyApplied and Environmental Microbiology
- 1 November 1998
Evidence that the enzyme responsible for cyanohydrin conversion is cyanide oxygenase is provided, providing the basis for a new mechanism of cyanide detoxification and assimilation in which keto acids play an essential role.
Alternative routes of enzymic cyanide metabolism in Pseudomonas fluorescens NCIMB 11764.
- D. Kunz, C. Wang, J. L. Chen
- BiologyMicrobiology
- 1 July 1994
Cell-free extracts from Pseudomonas fluorescens NCIMB 11764 catalysed the degradation of cyanide into products that included CO2, formic acid, formamide and ammonia, indicating that it is this enzyme that is most important in cyanide assimilation.
Deformation measurements on thin clay tactoids.
- D. Kunz, E. Max, R. Weinkamer, T. Lunkenbein, J. Breu, A. Fery
- Materials Science, MedicineSmall
- 17 August 2009
Catabolism of pseudocumene and 3-ethyltoluene by Pseudomonas putida (arvilla) mt-2: evidence for new functions of the TOL (pWWO) plasmid
- D. Kunz, P. Chapman
- Chemistry, BiologyJournal of Bacteriology
- 1 April 1981
Pseudocumene (1,2,4-trimethylbenzene) and 3-ethyltoluene were found to serve as growth substrates for Pseudomonas putida (arvilla) mt-2, in addition to toluene, m-xylene, and p-xylene as previously…
Cyanase-mediated utilization of cyanate in Pseudomonas fluorescens NCIB 11764
- D. Kunz, O. Nagappan
- BiologyApplied and Environmental Microbiology
- 1 January 1989
Enzymatic activity was shown to be bicarbonate dependent and specific for cyanate as a substrate, suggesting that cyanate utilization in this organism is facilitated by an enzyme resembling cyanase (cyanate amidohydrolase; EC 3.5.5).
Bacterial Cyanide Oxygenase Is a Suite of Enzymes Catalyzing the Scavenging and Adventitious Utilization of Cyanide as a Nitrogenous Growth Substrate
- R. Fernández, D. Kunz
- BiologyJournal of Bacteriology
- 15 September 2005
This is the first report describing the collective involvement of these four enzymes in the metabolic detoxification and utilization of CN as a bacterial nitrogenous growth substrate.
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