Untersuchungen zum Redox-System Bis-(pyridin-2,6-dicarbothioato)-ferrat(II) /-ferrat(III) [1]

1984 ◽  
Vol 39 (11) ◽  
pp. 1607-1613 ◽  
Author(s):  
U. Hildebrand ◽  
J. Lex ◽  
K. Taraz ◽  
S. Winkler ◽  
W. Ockels ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Redox Reactions ◽  
Culture Medium ◽  
Redox System ◽  
Blue Pigment

Abstract The structure of the blue pigment obtained from the culture medium of Pseudomonas putida upon addition of Fe++ and the nature of its redox reactions has been elucidated.

Dicyano-bis(pyridin-2,6-dicarbothioato)-ferrat (II)/ferrat (III), ein weiteres eisenhaltiges Redoxsystem aus der Kulturlösung eines Pseudomonas-Stammes [1] / Dicyano-bis(pyridin-2,6-dicarbothioato)-ferrate (II)/ferrate (III), a Further Fe Containing Redox System from the Culture Medium of Pseudomonas sp.

1985 ◽  
Vol 40 (3-4) ◽  
pp. 201-207 ◽  
Author(s):  
U. Hildebrand ◽  
K. Taraz ◽  
H. Budzikiewicz ◽  
H. Korth ◽  
G. Pulverer
Keyword(s):  
Pseudomonas Putida ◽  
Culture Medium ◽  
Redox System ◽  
Pseudomonas Sp ◽  
Redox Potentials ◽  
Bacterial Strains ◽  
Normal Potential

From the culture medium of Pseudomonas sp. a further Fe containing complex, viz. dicyano- bis(pyridin-2,6-dicarbothioato)-ferrate (III) (2) has been isolated which participates in a ferrate (II)/ferrate (III) redox system (normal potential of-0.013 V) in the range of the redox potentials of cytochromes. Pyridine-2,6-di(monothiocarboxylic acid) which originally has been considered to be characteristic for Pseudomonas putida has been found recently as a metabolite of other bacterial strains (two of which have been characterized in this paper) as well.

Selective synthetic methods using vanadium-mediated redox reactions

2005 ◽  
Vol 77 (9) ◽  
pp. 1539-1557 ◽  
Author(s):  
Toshikazu Hirao
Keyword(s):  
Lewis Acids ◽  
Redox Reactions ◽  
Radical Reaction ◽  
Redox System ◽  
Synthetic Methods ◽  
Pinacol Coupling ◽  
Oxidative Transformations ◽  
Low Valent

Oxovanadium(V) compounds serve as Lewis acids with oxidation capability and induce one-electron oxidative transformations of organosilicons, organotins, organoaluminums, organoborons, organozincs, and/or their ate complexes. Low-valent vanadium-catalyzed stereoselective reductive transformations, including dehalogenation, pinacol coupling, and the related radical reaction, have been developed by constructing a multicomponent redox system in combination with a coreductant and an additive.

Competitiveness in root colonization by Pseudomonas putida requires the rpoS gene

2001 ◽  
Vol 47 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Charles D Miller ◽  
Young-Cheol Kim ◽  
Anne J Anderson
Keyword(s):  
Pseudomonas Putida ◽  
Culture Medium ◽  
Wild Type Strain ◽  
Root Colonization ◽  
Plant Root ◽  
Wild Type ◽  
Rpos Gene ◽  
Activated Oxygen ◽  
Increased Sensitivity ◽  
Dose Dependent

The rpoS gene in Pseudomonas putida was essential for plant root colonization under competitive conditions from other microbes. The RpoS- mutant survived less well than the wild-type strain in culture medium, and unlike the wild-type, failed to colonize the roots in a peat matrix containing an established diverse microflora. The RpoS-deficient P. putida isolate was generated by insertion of a glucuronidase-npt cassette into the rpoS gene. The RpoS- mutant had dose-dependent increased sensitivity to oxidative stress and produced Mn-superoxide dismutase activity earlier than the parent. While extracts from wild-type P. putida stationary-phase cells contained three isozymes of catalase (CatA, CatB, and CatC), the σ38-deficient P. putida lacked CatB. These results are consistent with previous findings that CatB is induced in stationary-phase.Key words: catalase, starvation, activated oxygen species.

scholarly journals A Set of Genes Encoding a Second Toluene Efflux System in Pseudomonas putida DOT-T1E Is Linked to the tod Genes for Toluene Metabolism

2000 ◽  
Vol 182 (4) ◽  
pp. 937-943 ◽  
Author(s):  
Gilberto Mosqueda ◽  
Juan-Luis Ramos
Keyword(s):  
Pseudomonas Putida ◽  
Culture Medium ◽  
Efflux Pump ◽  
Site Directed Mutagenesis ◽  
Solvent Tolerance ◽  
Directed Mutagenesis ◽  
Wild Type ◽  
Efflux System ◽  
Host Chromosome ◽  
Knock Out

ABSTRACT Sequence analysis in Pseudomonas putida DOT-T1E revealed a second toluene efflux system for toluene metabolism encoded by the ttgDEF genes, which are adjacent to thetod genes. The ttgDEF genes were expressed in response to the presence of aromatic hydrocarbons such as toluene and styrene in the culture medium. To characterize the contribution of the TtgDEF system to toluene tolerance in P. putida, site-directed mutagenesis was used to knock out the gene in the wild-type DOT-T1E strain and in a mutant derivative, DOT-T1E-18. This mutant carried a Tn5 insertion in the ttgABCgene cluster, which encodes a toluene efflux pump that is synthesized constitutively. For site-directed mutagenesis, a cassette to knock out the ttgD gene and encoding resistance to tellurite was constructed in vitro and transferred to the corresponding host chromosome via the suicide plasmid pKNG101. Successful replacement of the wild-type sequences with the mutant cassette was confirmed by Southern hybridization. A single ttgD mutant, DOT-T1E-1, and a double mutant with knock outs in the ttgD andttgA genes, DOT-T1E-82, were obtained and characterized for toluene tolerance. This was assayed by the sudden addition of toluene (0.3% [vol/vol]) to the liquid culture medium of cells growing on Luria-Bertani (LB) medium (noninduced) or on LB medium with toluene supplied via the gas phase (induced). Induced cells of the singlettgD mutant were more sensitive to sudden toluene shock than were the wild-type cells; however, noninduced wild-type andttgD mutant cells were equally tolerant to toluene shock. Noninduced cells of the double DOT-T1E-82 mutant did not survive upon sudden toluene shock; however, they still remained viable upon sudden toluene shock if they had been previously induced. These results are discussed in the context of the use of multiple efflux pumps involved in solvent tolerance in P. putida DOT-T1E.

scholarly journals Identification of the Initial Steps in d-Lysine Catabolism in Pseudomonas putida

2007 ◽  
Vol 189 (7) ◽  
pp. 2787-2792 ◽  
Author(s):  
Olga Revelles ◽  
Rolf-Michael Wittich ◽  
Juan L. Ramos
Keyword(s):  
Pseudomonas Putida ◽  
Nitrogen Source ◽  
Culture Medium ◽  
Point Of View ◽  
Open Reading Frames ◽  
Gene Encoding ◽  
Carbon And Nitrogen ◽  
Extension Analysis ◽  
Reading Frames ◽  
Lysine Catabolism

ABSTRACT Pseudomonas putida uses l-lysine as the sole carbon and nitrogen source which preferentially requires its metabolism through two parallel pathways. In one of the pathways δ-aminovalerate is the key metabolite, whereas in the other l-lysine is racemized to d-lysine, and l-pipecolate and α-aminoadipate are the key metabolites. All the genes and enzymes involved in the d-lysine pathway, except for those involved in the conversion of d-lysine into Δ1-piperideine-2-carboxylate, have been identified previously (30). In this study we report that the conversion of d-lysine into Δ1-piperideine-2-carboxylate can be mediated by a d-lysine aminotransferase (PP3590) and a d-lysine dehydrogenase (PP3596). From a physiological point of view PP3596 plays a major role in the catabolism of d-lysine since its inactivation leads to a marked reduction in the growth rate with l- or d-lysine as the sole carbon and nitrogen source, whereas inactivation of PP3590 leads only to slowed growth. The gene encoding PP3590, called here amaC, forms an operon with dpkA, the gene encoding the enzyme involved in conversion of Δ1-piperideine-2-carboxylate to l-pipecolate in the d-lysine catabolic pathway. The gene encoding PP3596, called here amaD, is the fifth gene in an operon made up of seven open reading frames (ORFs) encoding PP3592 through PP3597. The dpkA amaC operon was transcribed divergently from the operon ORF3592 to ORF3597. Both promoters were mapped by primer extension analysis, which showed that the divergent −35 hexamers of these operon promoters were adjacent to each other. Transcription of both operons was induced in response to l- or d-lysine in the culture medium.

scholarly journals Effect of culture medium on biocalcification by Pseudomonas Putida, Lysinibacillus Sphaericus and Bacillus Subtilis

2011 ◽  
Vol 42 (2) ◽  
pp. 499-507 ◽  
Author(s):  
Márcia Aiko Shirakawa ◽  
Maria Alba Cincotto ◽  
Daniel Atencio ◽  
Christine C. Gaylarde ◽  
Vanderley M. John
Keyword(s):  
Bacillus Subtilis ◽  
Pseudomonas Putida ◽  
Culture Medium ◽  
Lysinibacillus Sphaericus

scholarly journals Electrochromic Properties and Electrochemical Behavior of Marennine, a Bioactive Blue-Green Pigment Produced by the Marine Diatom Haslea ostrearia

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 231
Author(s):  
Nellie Francezon ◽  
Mickaël Herbaut ◽  
Jean-François Bardeau ◽  
Charles Cougnon ◽  
William Bélanger ◽  
...  
Keyword(s):  
Redox System ◽  
Marine Diatom ◽  
Blue Pigment ◽  
Unstable State ◽  
Green Pigment ◽  
Haslea Ostrearia ◽  
Color Changes ◽  
Yellow Color ◽  
Food Applications ◽  
Molecular Structure Investigation

Marennine has long been known as the unique peculiar pigment responsible for the natural greening of oysters. It is specifically produced by the marine diatom Haslea ostrearia and it is a natural blue molecule indeed promising for food industry because of the rarity of such non-toxic, blue-colored pigments. In the search for its still not defined molecular structure, investigation of the color changes with the redox state has been carried out combining different approaches. Reducing and oxidizing chemicals have been added to purified marennine solutions and a stable blue-green color has been confirmed for the oxidized state, while a yellow color corresponded to the reduced unstable state. Raman spectroscopy has been used to monitor changes in the Raman spectra corresponding to the different colored states, and cyclic voltammetry has allowed the detection of a redox system in which protons and electrons are exchanged. These findings show that marennine is a suitable stable blue pigment for use in food applications and help in the elucidation of the chromophore structure.

Weitere aus dem Kulturmedium von Pseudomonas putida isolierte Pyridinderivate -Genuine Metaboliten oder Artefakte ?/Further Pyridine Derivatives Isolated from the Culture Medium of Pseudomonas putida - Genuine Metabolites or Artefacts ?

1983 ◽  
Vol 38 (4) ◽  
pp. 516-520 ◽  
Author(s):  
H. Budzikiewicz ◽  
U. Hildebrand ◽  
W. Ockels ◽  
M. Reiche ◽  
K. Taraz
Keyword(s):  
Methyl Ester ◽  
Pseudomonas Putida ◽  
Culture Medium ◽  
Pyridine Derivatives

Abstract From the culture medium of Pseudomonas putida after treatment with CH2N2 besides the expected Pyridine-2,6-di(monothiocarboxylic acid)-di-S-methyl ester a series of pyridine derivatives could be isolated which could be shown to be artefacts formed from pyridine-2,6-di(monothiocarboxylic acid).

[(Methoxythio)carbonyl]pyridin-Derivate, eine neue Verbindungsklasse aus Pseudomonas putida [1] / [(M ethoxythio)carbonyl]pyridine Derivatives, a New Class of Compounds from Pseudomonas putida [1]

1985 ◽  
Vol 40 (11) ◽  
pp. 1563-1565 ◽  
Author(s):  
U. Hildebrand ◽  
K. Taraz ◽  
H. Budzikiewicz
Keyword(s):  
Pseudomonas Putida ◽  
Structure Elucidation ◽  
Culture Medium ◽  
Pyridine Derivatives ◽  
New Class

From the culture medium of Pseudomonas putida three pyridine derivatives were isolated which contain the (methoxythio)carbonyl (CO−S-OCH3) group thus far not described in the literature. Characterization and structure elucidation are reported.

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