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Results: 1-8 |
Results: 8
Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization
Authors: Parschat, K Canne, C Huttermann, J Kappl, R Fetzner, S
Citation: K. Parschat et al., Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization, BBA-PROT ST, 1544(1-2), 2001, pp. 151-165
Site-directed mutagenesis of potential catalytic residues in 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, and hypothesis on the catalytic mechanism of 2,4-dioxygenolytic ring cleavage
Authors: Fischer, F Fetzner, S
Citation: F. Fischer et S. Fetzner, Site-directed mutagenesis of potential catalytic residues in 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, and hypothesis on the catalytic mechanism of 2,4-dioxygenolytic ring cleavage, FEMS MICROB, 190(1), 2000, pp. 21-27
Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: Molybdenum hydroxylases and ring-opening 2,4-dioxygenases
Authors: Fetzner, S
Citation: S. Fetzner, Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: Molybdenum hydroxylases and ring-opening 2,4-dioxygenases, NATURWISSEN, 87(2), 2000, pp. 59-69
Bioconversion of pyrimidine by resting cells of quinoline-degrading bacteria
Authors: Fetzner, S
Citation: S. Fetzner, Bioconversion of pyrimidine by resting cells of quinoline-degrading bacteria, FEMS MICROB, 176(2), 1999, pp. 291-299
Cloning, sequence analysis; and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase
Authors: Max, N Betz, A Facey, S Lingens, F Hauer, B Fetzner, S
Citation: N. Max et al., Cloning, sequence analysis; and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase, BBA-PROT ST, 1431(2), 1999, pp. 547-552
Bacterial 2,4-dioxygenases: New members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases
Authors: Fischer, F Kunne, S Fetzner, S
Citation: F. Fischer et al., Bacterial 2,4-dioxygenases: New members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases, J BACT, 181(18), 1999, pp. 5725-5733
Flavonol 2,4-dioxygenase from Aspergillus niger DSM 821, a type 2 Cu-II-containing glycoprotein
Authors: Hund, HK Breuer, J Lingens, F Huttermann, J Kappl, R Fetzner, S
Citation: Hk. Hund et al., Flavonol 2,4-dioxygenase from Aspergillus niger DSM 821, a type 2 Cu-II-containing glycoprotein, EUR J BIOCH, 263(3), 1999, pp. 871-878
Bacterial dehalogenation
Authors: Fetzner, S
Citation: S. Fetzner, Bacterial dehalogenation, APPL MICR B, 50(6), 1998, pp. 633-657
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