ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    A novel metabolite in the microbial degradation of 2-chlorobenzoate
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 161 (1989), S. 700-705 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0006-291X(89)92656-9
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    EPR, ESEEM and endor study of 2Fe2S-centers. A comparison of rieske- and ferredoxin-type clusters.
    Amsterdam : Elsevier
    Journal of Inorganic Biochemistry 56 (1994), S. 27 
    Details
    ISSN: 0162-0134
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0162-0134(94)85068-2
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Degradation of benzoate via benzoyl-coenzyme A and gentisate by Bacillus stearothermophilus PK1, and purification of gentisate 1,2-dioxygenase (1996)
    Springer
    Biology and fertility of soils 23 (1996), S. 307-313 
    Details
    ISSN: 1432-0789
    Keywords: Bacillus stearothermophilus ; Benzoate degradation ; Benzoyl-coenzyme A ; Gentisate 1,2-dioxygenase ; Thermophils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The thermophilic Bacillus stearothermophilus PK1 utilized benzoate, 3-hydroxybenzoate, and gentisate as sole source of carbon and energy. 2- and 4-Hydroxybenzoate, 2,3- and 3,4-dihydroxybenzoate, and catechol did not support growth. Degradation of benzoate proceeded via benzoyl-coenzyme A (benzoyl-CoA) and gentisate. The inducible benzoyl-CoA ligase converted benzoate but not 3-hydroxybenzoate to its coenzyme A thioester. Gentisate 1,2-dioxygenase from B. stearothermophilus PK1 was purified to homogeneity. The enzyme is presumed to be a homohexamer with a subunit molecular mass of 40 kDa. It showed maximal activity at 65–70°C. After incubation for 80 min at 65°C, 50% of the original activity was lost. Gentisate 1,2-dioxygenase activity from strain PK1 was strictly dependent on exogenously added Fe2+, and it was inhibited by metal-chelating agents, indicating an essential role of Fe2+ in catalysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00335959
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Degradation of benzoate via benzoyl-coenzyme A and gentisate by Bacillus stearothermophilus PK1, and purification of gentisate 1,2-dioxygenase (1996)
    Springer
    Biology and fertility of soils 23 (1996), S. 307-313 
    Details
    ISSN: 1432-0789
    Keywords: Key wordsBacillus stearothermophilus ; Benzoate ; degradation ; Benzoyl-coenzyme A ; Gentisate 1 ; 2-dioxygenase ; Thermophils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The thermophilic Bacillus stearothermophilus PK1 utilized benzoate, 3-hydroxybenzoate, and gentisate as sole source of carbon and energy. 2- and 4-Hydroxybenzoate, 2,3- and 3,4-dihydroxybenzoate, and catechol did not support growth. Degradation of benzoate proceeded via benzoyl-coenzyme A (benzoyl-CoA) and gentisate. The inducible benzoyl-CoA ligase converted benzoate but not 3-hydroxybenzoate to its coenzyme A thioester. Gentisate 1,2-dioxygenase from B. stearothermophilus PK1 was purified to homogeneity. The enzyme is presumed to be a homohexamer with a subunit molecular mass of 40 kDa. It showed maximal activity at 65–70°C. After incubation for 80 min at 65°C, 50% of the original activity was lost. Gentisate 1,2-dioxygenase activity from strain PK1 was strictly dependent on exogenously added Fe2+, and it was inhibited by metal-chelating agents, indicating an essential role of Fe2+ in catalysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00335959
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions (1998)
    Springer
    Applied microbiology and biotechnology 49 (1998), S. 237-250 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Bacteria have evolved a diverse potential to transform and even mineralize numerous organic compounds of both natural and xenobiotic origin. This article describes the occurrence of N-heteroaromatic compounds and presents a review of the bacterial degradation of pyridine and its derivatives, indole, isoquinoline, and quinoline and its derivatives. The bacterial metabolism of these compounds under different redox conditions – by aerobic, nitrate-reducing, sulfate-reducing and methanogenic bacteria – is discussed. However, in natural habitats, various environmental factors, such as sorption phenomena, also influence bacterial conversion processes. Thus, both laboratory and field studies are necessary to aid our understanding of biodegradation in natural ecosystems and assist the development of strategies for bioremediation of polluted sites. Occurring predominantly near (former) wood-treatment facilities, creosote is a frequent contaminant of soil, subsoil, groundwater, and aquifer sediments. In situ as well as withdrawal-and-treatment techniques have been designed to remediate such sites, which are polluted with complex mixtures of aromatic and heterocyclic compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051164
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Bacterial dehalogenation (1998)
    Springer
    Applied microbiology and biotechnology 50 (1998), S. 633-657 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Halogenated organic compounds are produced industrially in large quantities and represent an important class of environmental pollutants. However, an abundance of haloorganic compounds is also produced naturally. Bacteria have evolved several strategies for the enzyme-catalyzed dehalogenation and degradation of both haloaliphatic and haloaromatic compounds: (i) Oxidative dehalogenation is the result of mono- or dioxygenase-catalyzed, co-metabolic or metabolic reactions. (ii) In dehydrohalogenase-catalyzed dehalogenation, halide elimination leads to the formation of a double bond. (iii) Substitutive dehalogenation in most cases is a hydrolytic process, catalyzed by halidohydrolases, but there also is a “thiolytic” mechanism with glutathione as cosubstrate. Dehalogenation by halohydrin hydrogen-halide lyases is the result of an intramolecular substitution reaction. (iv) A distinct dechlorination mechanism involves methyl transfer from chloromethane onto tetrahydrofolate. (v) Reductive dehalogenations are co-metabolic processes, or they are specific reactions involved in substrate utilization (carbon metabolism), or reductive dehalogenation is coupled to energy conservation: some anaerobic bacteria use a specific haloorganic compound as electron acceptor of a respiratory process. This review discusses the mechanisms of enzyme-catalyzed dehalogenation reactions, describes some pathways of the bacterial degradation of haloorganic compounds, and indicates some trends in the biological treatment of organohalogen-polluted air, groundwater, soil, and sediments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051346
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Enzymes Involved in the Aerobic Bacterial Degradation of N-Heteroaromatic Compounds: Molybdenum Hydroxylases and Ring-Opening 2,4-Dioxygenases (2000)
    Springer
    Naturwissenschaften 87 (2000), S. 59-69 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Notes: N -heteroaromatic compounds are utilized by micro-organisms as a source of carbon (and nitrogen) and energy. The aerobic bacterial degradation of these growth substrates frequently involves several hydroxylation steps and subsequent dioxygenolytic cleavage of (di)hydroxy-substituted heteroaromatic intermediates to aliphatic metabolites which finally are channeled into central metabolic pathways. As a rule, the initial bacterial hydroxylation of a N-heteroaromatic compound is catalyzed by a molybdenum hydroxylase, which uses a water molecule as source of the incorporated oxygen. The enzyme's redox-active centers – the active site molybdenum ion coordinated to a distinct pyranopterin cofactor, two different [2Fe2S] centers, and in most cases, flavin adenine dinucleotide – transfer electrons from the N-heterocyclic substrate to an electron acceptor, which for many molybdenum hydroxylases is still unknown. Ring-opening 2,4-dioxygenases involved in the bacterial degradation of quinaldine and 1H-4-oxoquinoline catalyze the cleavage of two carbon-carbon bonds with concomitant formation of carbon monoxide. Since they contain neither a metal center nor an organic cofactor, and since they do not show any sequence similarity to known oxygenases, these unique dioxygenases form a separate enzyme family. Quite surprisingly, however, they appear to be structurally and mechanistically related to enzymes of the α/β hydrolase fold superfamily. Microbial enzymes are a great resource for biotechnological applications. Microbial strains or their enzymes may be used for degradative (bioremediation) or synthetic (biotransformation) purposes. Modern bioremediation or biotransformation strategies may even involve microbial catalysts or strains designed by protein engineering or pathway engineering. Prerequisite for developing such modern tools of biotechnology is a comprehensive understanding of microbial metabolic pathways, of the structure and function of enzymes, and of the molecular mechanisms of biocatalysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001140050011
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    facet.materialart.
    Unknown
    Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions (1998)
    Springer
    Details
    Publication Date: 1998-03-27
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    Bacterial dehalogenation (1998)
    Springer
    Details
    Publication Date: 1998-12-16
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    Degradation of benzoate via benzoyl-coenzyme A and gentisate by Bacillus stearothermophilus PK1, and purification of gentisate 1,2-dioxygenase (1996)
    Springer
    Details
    Publication Date: 1996-10-01
    Print ISSN: 0178-2762
    Electronic ISSN: 1432-0789
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...