Academics at the Department of Biology

Wissenschaftlicher Werdegang
- 1982- 1988 Studium der Biologie (Diplom)
- 1990 Promotion zum Dr. rer. nat., Universität Hohenheim
- 1996 Habilitation in Mikrobiologie, Universität Hohenheim
- 1996-2002 Vertretung der Professur für Mikrobiologie an der Carl von Ossietzky Universität Oldenburg
- seit 2002 Professorin für Mikrobiologie am Institut für Molekulare Mikrobiologie und Biotechnologie der WWU Münster

Lehrschwerpunkte

- Mikrobiologie
- Bakterielle Stoffwechselphysiologie
- Enzymbiochemie und Enzymbiotechnologie
Forschungsschwerpunkte
- Enzymbiochemie und -biotechnologie: Oxygenasen, Hydrolasen.
- Bakterieller Stoffwechsel von Heteroaromaten: Abbauwege und deren Regulation;
lineare Abbauplasmide.
http://www.uni-muenster.de/Biologie.IMMB.Fetzner/en/Lehre/index.html

ausgewählte Projekte
Ring-cleaving dioxygenases: cofactor-independent versus metal-containing enzymes
(Support: DFG)
2,4-Dioxygenases that catalyze the cleavage of 3-hydroxy-4(1H)quinolones to carbon monoxide and N-alkylanthranilate are cofactor-independent oxygenases with an α/β-hydrolase fold. Steady-state and transient kinetics studies are being performed to obtain insight into the kinetic parameters and the time-dependent microscopic pathway of the reaction. The overall goal of the project is to contribute to a comprehensive understanding of how cofactor-free oxygenases work.
Flavonol dioxygenases also catalyze the cleavage of two carbon-carbon bonds with release of carbon monoxide, but depend on a divalent metal ion for catalysis. This raises the question of whether CO-forming dioxygenases have evolved fundamentally different ways to catalyze a similar reaction, or whether there are close mechanistic similarities of metal-dependent and cofactor-independent enzymes. Comparison of kinetic, spectroscopic and structural properties of different metal forms of flavonol dioxygenase with the properties of cofactor-independent dioxygenases will contribute to enlighten similarities and differences of the respective reaction mechanisms.

Bacterial metabolism of 2-methylquinoline and naturally occurring 2-alkyl-4(1H)quinolones
(Support: DFG)
2-Methylquinoline degradation by Arthrobacter nitroguajacolicus Rü61a to anthranilate is encoded by operons located on the linear plasmid pAL1. Anthranilate can be degraded via a chromosomal catechol pathway, however, another operon of pAL1 was proposed to encode enzymes for anthranilate conversion via coenzyme A intermediates. The project aims at characterizing the transcriptional regulation of catabolic operons of pAL1.
We also address the question of how bacteria degrade naturally occurring alkylquinolones, such as 2-heptyl-4(1H)quinolone and 2-heptyl-3-hydroxy-4(1H)quinolone, which are important quorum sensing signalling molecules of Pseudomonas aeruginosa. The goal is to identify novel enzymes for the inactivation of these compounds.


Ausgewählte Kooperationen
- Prof. Dr. H. Dobbek, Bayreuth: Kristallstruktur von Metalloenzymen
- Prof. Dr. H.-J. Hinz, Biophysikalische Chemie, WWU Münster: Strukturbildung und Stabilität von Cofaktor-unabhängigen Dioxygenasen
- Dr. R. Kappl, Universität des Saarlandes: ESR-Spektroskopie an Enzymen
- Dr. R. Steiner, London: Kristallstruktur Cofaktor-unabhängiger Dioxygenasen
- Prof. Dr. U. Wagner, Graz: Struktur und Funktion von Hydrolasen
- Prof. Dr. P. Williams, Nottingham: Bakterieller Stoffwechsel von Alkylchinolonen.

Publications

  • Drees SL, Li C, Prasetya F, Saleem M, Dreveny I, Williams P, Hennecke U, Emsley J, Fetzner S. . ‘PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism.’ Journal of Biological Chemsitry Jan 25, 2016 pii: jbc.M115.708453. [Epub ahead of print].
  • Tettmann B., Niewerth C., Kirschhöfer F., Neidig A., Dötsch A., Brenner-Weiss G., Fetzner S., Overhage J. . ‘Enzyme-mediated quenching of the Pseudomonas Quinolone Signal (PQS) promotes biofilm formation of pseudomonas aeruginosa by increasing iron availability.’ Frontiers in Microbiology 7, No. null. doi: 10.3389/fmicb.2016.01978.
  • Zender M., Witzgall F., Drees S., Weidel E., Maurer C., Fetzner S., Blankenfeldt W., Empting M., Hartmann R. . ‘Dissecting the Multiple Roles of PqsE in Pseudomonas aeruginosa Virulence by Discovery of Small Tool Compounds.’ ACS Chemical Biology 11, No. 6: 1755-1763. doi: 10.1021/acschembio.6b00156.
  • Jeoung J., Nianios D., Fetzner S., Dobbek H. . ‘Quercetin 2,4-Dioxygenase Activates Dioxygen in a Side-On O2-Ni Complex.’ Angewandte Chemie - International Edition 55, No. 10: 3281-3284. doi: 10.1002/anie.201510741.
  • Birmes F., Fetzner S. . „Bakterielle Kommunikation: Signale und Signal-inaktivierende Enzyme.“ BioSpektrum 22, No. 3: 251-254. doi: 10.1007/s12268-016-0681-4.
  • Müller C., Birmes F., Rückert C., Kalinowski J., Fetzner S. . ‘Rhodococcus erythropolis BG43 genes mediating Pseudomonas aeruginosa quinolone signal degradation and virulence factor attenuation.’ Applied and Environmental Microbiology 81, No. 22: 7720-7729. doi: 10.1128/AEM.02145-15.
  • Rückert C., Birmes F., Müller C., Niewerth H., Winkler A., Fetzner S., Kalinowski J. . ‘Complete genome sequence of Rhodococcus erythropolis BG43 (DSM 46869), a degrader of Pseudomonas aeruginosa quorum sensing signal molecules.’ Journal of Biotechnology 211, No. null: 99-100. doi: 10.1016/j.jbiotec.2015.07.014.
  • Drees S., Fetzner S. . ‘PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules.’ Chemistry and Biology 22, No. 5: 611-618. doi: 10.1016/j.chembiol.2015.04.012.
  • Nianios D., Thierbach S., Steimer L., Lulchev P., Klostermeier D., Fetzner S. . ‘Nickel quercetinase, a "promiscuous" metalloenzyme: Metal incorporation and metal ligand substitution studies Protein and enzyme biochemistry.’ BMC Biochemistry 16, No. 1. doi: 10.1186/s12858-015-0039-4.
  • Soh E., Chhabra S., Halliday N., Heeb S., Müller C., Birmes F., Fetzner S., Cámara M., Chan K., Williams P. . ‘Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule.’ Environmental Microbiology null, No. null. doi: 10.1111/1462-2920.12857. [In Press]
  • Fetzner S. . ‘Quorum quenching enzymes.’ J. Biotechnol. 201: 2-14.
  • Wagner,Ulrike Gabriella U.G.,Dimaio,Frank P. F.P.,Kolkenbrock,Stephan S.,Fetzner,Susanne S.,. . ‘Crystal structure analysis of EstA from Arthrobacter sp. Rue61a - An insight into catalytic promiscuity.’ FEBS Letters 588, No. 7: 1154-1160. doi: 10.1016/j.febslet.2014.02.045.
  • Müller, Christine; Birmes, Franziska; Niewerth, Heiko; Fetzner, Susanne. . ‘Conversion of the Pseudomonas aeruginosa quinolone signal and related alkylhydroxyquinolines by Rhodococcus sp. strain BG43.’ Applied and Environmental Microbiology 80, No. 23: 7266-7274. doi: 10.1128/AEM.02342-14.
  • Niewerth H., Parschat K., Rauschenberg M., Ravoo B.J., Fetzner S. . ‘The PaaX-Type Repressor MeqR2 of Arthrobacter sp. Strain Rue61a, Involved in the Regulation of Quinaldine Catabolism, Binds to Its Own Promoter and to Catabolic Promoters and Specifically Responds to Anthraniloyl Coenzyme A.’ Journal of Bacteriology 195, No. 5: 1068-1080. doi: 10.1128/JB.01547-12.
  • Thierbach S, Bui N, Zapp J, Chhabra SR, Kappl R, Fetzner S. . ‘Substrate-Assisted O2 Activation in a Cofactor-Independent Dioxygenase.’ Chemistry & Biology 21: 217-225. doi: 10.1016/j.chembiol.2013.11.013.
  • Vila-Sanjurjo C., Fuenzalida J., Menchicchi B., Engwer C., Hoffman S., Pereira S., Remunan-Lopez C., Alonso M., Vidal A., Moerschbacher B., Kollenbrock S., Fetzner S., Philipp B., Goycoolea F. . ‘Chitosan-based nanomaterials for drug delivery and antibiotic-free bacterial control.’Contributed to the Nanotechnology 2013: Bio Sensors, Instruments, Medical, Environment and Energy - 2013 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2013, Washington, DC, usa.
  • Fetzner S., Drees S.L. . ‘Old molecules, new biochemistry.’ Chemistry and Biology 20, No. 12: 1438-1440. doi: 10.1016/j.chembiol.2013.12.001.
  • Thierbach S, Büldt-Karentzopoulos K, Dreiling A, Hennecke U, König S, Fetzner S. . ‘Hydrolase-like properties of a cofactor-independent dioxygenase.Chembiochem 13, No. 8: 1125-7. doi: 10.1002/cbic.201200152.
  • Kolkenbrock S, Naumann B, Hippler M, Fetzner S. . ‘A Novel Replicative Enzyme Encoded by the Linear Arthrobacter Plasmid pAL1.’ JOURNAL OF BACTERIOLOGY 192, No. 19: 4935-4943. doi: 10.1128/JB.00614-10.
  • Fetzner S, Steiner RA. . ‘Cofactor-independent oxidases and oxygenases.’ APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 86, No. 3: 791-804. doi: 10.1007/s00253-010-2455-0.
  • Kolkenbrock S, Fetzner S. . ‘Identification and in vitro deoxynucleotidylation of the terminal protein of the linear plasmid pAL1 of Arthrobacter nitroguajacolicus Ru61a.’ FEMS MICROBIOLOGY LETTERS 304, No. 2: 169-176. doi: 10.1111/j.1574-6968.2010.01900.x.
  • Steiner RA, Janssen HJ, Roversi P, Oakley AJ, Fetzner S. . ‘Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold.’ PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AME 107, No. 2: 657-662. doi: 10.1073/pnas.0909033107.
  • Fetzner Susanne. . ‘Aerobic degradation of halogenated aliphatics.’ In Handbook of Hydrocarbon and Lipid Microbiology, Part 10: Biochemsitry of Aerobic Degradation, edited by Timmis, KN (Eds.): .: Springer. doi: 10.1007/978-3-540-77587-1_62.
  • Pustelny C, Albers A, Buldt-Karentzopoulos K, Parschat K, Chhabra SR, Camara M, Williams P, Fetzner S. . ‘Dioxygenase-Mediated Quenching of Quinolone-Dependent Quorum Sensing in Pseudomonas aeruginosa.’ CHEMISTRY & BIOLOGY 16, No. 12: 1259-1267. doi: 10.1016/j.chembiol.2009.11.013.
  • Merkens H, Kappl R, Jakob RP, Schmid FX, Fetzner S. . ‘Quercetinase QueD of Streptomyces sp FLA, a Monocupin Dioxygenase with a Preference for Nickel and Cobalt.’ BIOCHEMISTRY 47, No. 46: 12185-12196. doi: 10.1021/bi801398x.
  • Merkens H, Fetzner S. . ‘Transcriptional analysis of the queD gene coding for quercetinase of Streptomyces sp FLA.’ FEMS MICROBIOLOGY LETTERS 287, No. 1: 100-107. doi: 10.1111/j.1574-6968.2008.01296.x.
  • Boehm K, Guddorf J, Albers A, Kamiyama T, Fetzner S, Hinz HJ. . ‘Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism.’ BIOCHEMISTRY 47, No. 27: 7116-7126. doi: 10.1021/bi800554v.
  • Fetzner S. . ‘Cofactor-independent oxygenases go it alone.’ NATURE CHEMICAL BIOLOGY 3, No. 7: 374-375. doi: 10.1038/nchembio0707-374.
  • Merkens H, Sielker S, Rose K, Fetzner S. . ‘A new monocupin quercetinase of Streptomyces sp FLA: identification and heterologous expression of the queD gene and activity of the recombinant enzyme towards different flavonols.’ ARCHIVES OF MICROBIOLOGY 187, No. 6: 475-487. doi: 10.1007/s00203-007-0215-z.
  • Kolkenbrock S, Parschat K, Beermann B, Hinz HJ, Fetzner S. . N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Ru61a, an alpha/beta-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant (vol 188, pg 8430, 2006). doi: 10.1128/JB.00325-07.
  • Steiner RA, Frerichs-Deeken U, Fetzner S. . ‘Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily.’ ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COM 63: 382-385. doi: 10.1107/S174430910701353X.
  • Parschat K, Overhage J, Strittmatter AW, Henne A, Gottschalk G, Fetzner S. . ‘Complete nucleotide sequence of the 113-kilobase linear catabolic plasmid pAL1 of Arthrobacter nitroguajacolicus Ru61a and transcriptional analysis of genes involved in quinaldine degradation.’ JOURNAL OF BACTERIOLOGY 189, No. 10: 3855-3867. doi: 10.1128/JB.00089-07.
  • Qi R, Fetzner S, Oakley AJ. . ‘Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family.’ ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COM 63: 378-381. doi: 10.1107/S1744309107013760.
  • Beermann B, Guddorf J, Boehm K, Albers A, Kolkenbrock S, Fetzner S, Hinz HJ. . ‘Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase.’ BIOCHEMISTRY 46, No. 14: 4241-4249. doi: 10.1021/bi0622423.
  • Schutte M, Fetzner S. . ‘EstA from Arthrobacter nitroguajacolicus Ru61a, a thermo- and solvent-tolerant carboxylesterase related to class C beta-lactamases.’ CURRENT MICROBIOLOGY 54, No. 3: 230-236. doi: 10.1007/s00284-006-0438-2.
  • Fetzner Susanne, Kolkenbrock Stephan, Parschat Katja. . ‘Catabolic linear plasmids.’ In Microbial linear plasmids, edited by Meinhardt F, Klassen R (Eds.): , 63-98.: Springer.
  • Kolkenbrock S, Parschat K, Beermann B, Hinz HJ, Fetzner S. . ‘N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Ru61a, an alpha/beta-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant.’ JOURNAL OF BACTERIOLOGY 188, No. 24: 8430-8440. doi: 10.1128/JB.01085-06.
  • Kappl R, Sielker S, Ranguelova K, Wegner J, Parschat K, Huttermann J, Fetzner S. . ‘Spectroscopic and biochemical studies on protein variants of quinaldine 4-oxidase: Role of E736 in catalysis and effects of serine ligands on the FeSI and FeSII clusters.’ BIOCHEMISTRY 45, No. 49: 14853-14868. doi: 10.1021/bi061185a.
  • Rose K, Fetzner S. . ‘Identification of linear plasmid pAM1 in the flavonoid degrading strain Actinoplanes missouriensis(T) (DSM 43046).’ PLASMID 55, No. 3: 249-254. doi: 10.1016/j.plasmid.2005.10.003.
  • Carl B, Fetzner S. . ‘Transcriptional activation of quinoline degradation operons of Pseudomonas putida 86 by the AraC/XylS-type regulator OxoS and cross-regulation of the PqorM promoter by XylS.’ APPLIED AND ENVIRONMENTAL MICROBIOLOGY 71, No. 12: 8618-8626. doi: 10.1128/AEM.71.12.8618-8626.2005.
  • Frerichs-Deeken U, Fetzner S. . ‘Dioxygenases without requirement for cofactors: Identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase.’ CURRENT MICROBIOLOGY 51, No. 5: 344-352. doi: 10.1007/s00284-005-0065-3.
  • Purvanov V, Fetzner S. . ‘Replacement of active-site residues of quinoline 2-oxidoreductase involved in substrate recognition and specificity.’ CURRENT MICROBIOLOGY 50, No. 4: 217-222. doi: 10.1007/s00284-004-4452-y.
  • Overhage J, Sielker S, Homburg S, Parschat K, Fetzner S. . ‘Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate.’ MICROBIOLOGY-SGM 151: 491-500. doi: 10.1099/mic.0.27521-0.
  • Boer DR, Muller A, Fetzner S, Lowe DJ, Romao MJ. . ‘On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7.’ ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COM 61: 137-140.
  • Frerichs-Deeken U, Ranguelova K, Kappl R, Huttermann J, Fetzner S. . ‘Dioxygenases without requirement for cofactors and their chemical model reaction: Compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion.’ BIOCHEMISTRY 43, No. 45: 14485-14499. doi: 10.1021/bi048735u.
  • Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H. . ‘Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.’ STRUCTURE 12, No. 8: 1425-1435. doi: 10.1016/j.str.2004.05.014.
  • Carl B, Arnold A, Hauer B, Fetzner S. . ‘Sequence and transcriptional analysis of a gene cluster of Pseudomonas putida 86 involved in quinoline degradation.’ GENE 331: 177-188. doi: 10.1016/j.gene.2004.02.020.
  • Parschat K, Hauer B, Kappl R, Kraft R, Huttermann J, Fetzner S. . ‘Gene cluster of Arthrobacter ilicis Ru61a involved in the degradation of quinaldine to anthranilate.’ JOURNAL OF BIOLOGICAL CHEMISTRY 278, No. 30: 27483-27494. doi: 10.1074/jbc.M301330200.
  • Frerichs-Deeken U, Goldenstedt B, Gahl-Janssen R, Kappl R, Huttermann J, Fetzner S. . ‘Functional expression of the quinoline 2-oxidoreductase genes (qorMSL) in Pseudomonas putida KT2440 pUF1 and in P-putida 86-1 Delta qor pUF1 and analysis of the Qor proteins.’ EUROPEAN JOURNAL OF BIOCHEMISTRY 270, No. 7: 1567-1577. doi: 10.1046/j.1432-1033.2003.03526.x.
  • Andreesen JR, Fetzner S. . ‘The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine.’, edited by (Ed.): , 405-430.
  • Berthe-Corti L, Fetzner S. . ‘Bacterial metabolism of n-alkanes and ammonia under oxic, suboxic and anoxic conditions.’ ACTA BIOTECHNOLOGICA 22, No. 3-4: 299-336. doi: 10.1002/1521-3846(200207)22:3/4299::AID-ABIO299>3.0.CO;2-F.
  • Kappl R, Huttermann J, Fetzner S. . ‘The molybdenum-containing hydroxylases of quinoline, isoquinoline, and quinaldine.’, edited by (Ed.): , 481-537.
  • Fetzner S. . ‘Oxygenases without requirement for cofactors or metal ions.’ APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 60, No. 3: 243-257.
  • Israel I, Sohni M, Fetzner S. . ‘Expression of the iorAB genes from Brevundimonas diminuta 7 encoding the molybdenum hydroxylase isoquinoline 1-oxidoreductase in Pseudomonas putida.’ FEMS MICROBIOLOGY LETTERS 210, No. 1: 123-127. doi: 10.1111/j.1574-6968.2002.tb11170.x.
  • Fetzner S. . ‘Biodegradation of Xenobiotics.’ In Encyclopedia of Life Support Systems, edited by Doelle, Da Silva (Eds.): . Oxford, UK: Eolss Publishers.
  • Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S. . ‘Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization.’ BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY 1544, No. 1-2: 151-165. doi: 10.1016/S0167-4838(00)00214-4.
  • Fischer F, Fetzner S. . ‘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 MICROBIOLOGY LETTERS 190, No. 1: 21-27. doi: 10.1111/j.1574-6968.2000.tb09256.x.
  • Fetzner S. . ‘Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: Molybdenum hydroxylases and ring-opening 2,4-dioxygenases.’ NATURWISSENSCHAFTEN 87, No. 2: 59-69. doi: 10.1007/s001140050011.
  • Fischer F, Künne S, Fetzner S. . ‘Bacterial 2,4-dioxygenases: New members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.’ Journal of Bacteriology 181: 5725-5733.
  • Max N, Betz A, Facey S, Lingens F, Hauer B, Fetzner S. . ‘Cloning, sequence analysis, and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxo-quinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase.’ Biochimica et Biophysica Acta 1431: 547-552.
  • Hund H, Breuer J, Lingens F, Hüttermann J, Kappl R, Fetzner S. . ‘Flavonol 2,4-dioxygenase from Aspergillus niger DSM 821, a type 2–CuII-containing glycoprotein.’ European Journal of Biochemistry 263: 871-878.
  • Fetzner S. . ‘Bioconversion of pyrimidine by resting cells of quinoline-degrading bacteria.’ FEMS Microbiology Letters 176: 291-299.
  • Canne C, Lowe DJ, Fetzner S, Adams B, Smith AT, Kappl R, Bray RC, Hüttermann J. . ‘Kinetics and interactions of molybdenum and iron-sulfur centres in bacterial enzymes of the xanthine oxidase family: Mechanistic implications.’ Biochemistry 38: 14077-14087.
  • Fetzner S. . ‘Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions.’ Applied Microbiology and Biotechnology 49: 237-250.
  • Fetzner S, Tshisuaka B, Lingens F, Kappl R, Hüttermann, J. . ‘Bacterial degradation of quinoline and -derivatives - pathways and their biocatalysts.’ Angewandte Chemie (International Edition) 37.
  • Fetzner S. . ‘Bacterial dehalogenation.’ Applied Microbiology and Biotechnology 50: 633-657.
  • Rosche B, Tshisuaka B, Hauer B, Lingens F, Fetzner S. . ‘2-Oxo-1,2-dihydro-quinoline 8-monooxygenase: Phylogenetic relationship to other multicomponent non-heme iron oxygenases.’ Journal of Bacteriology 179: 3549-3554.
  • Canne C, Stephan I, Finsterbusch J, Lingens F, Kappl R, Fetzner S, Hüttermann J. . ‘Comparative EPR and redox studies of three prokaryotic enzymes of the xanthine oxidase family: quinoline 2-oxidoreductase, quinaldine 4-oxidase, and isoquinoline 1-oxidoreductase.’ Biochemistry 36: 9780-9790.
  • Stephan I, Tshisuaka B, Fetzner S, Lingens F. . ‘Quinaldine 4-oxidase from Arthrobacter sp. Rü61a. A versatile procaryotic molybdenum-containing hydroxylase active towards N-heterocycles and aromatic aldehydes.’ European Journal of Biochemistry 236: 155-162.
  • Bubeck B, Tshisuaka B, Fetzner S, Lingens F. . ‘Hydroxylation of quinaldic acid: Quinaldic acid 4-monooxygenase from Alcaligenes sp. F2 versus quinaldic acid 4-oxidoreductases.’ Biochimica et Biophysica Acta 1293: 39-44.
  • Bläse M, Bruntner C, Tshisuaka B, Fetzner S, Lingens F. . ‘Cloning, expression, and sequence analysis of the three genes encoding quinoline 2-oxidoreductase, a molybdenum-containing hydroxylase from Pseudomonas putida 86.’ Journal of Biological Chemistry 271: 23068-23079.
  • Bauer I, Max N, Fetzner S, Lingens F. . ‘2,4-Dioxygenases catalyzing N-heterocyclic ring cleavage and formation of carbon monoxide.’ European Journal of Biochemistry 240: 576-583.
  • Kiemer P, Tshisuaka B, Fetzner S, Lingens F. . ‘Degradation of benzoate via benzoyl-coenzyme A and gentisate by Bacillus stearothermophilus PK1, and purification of gentisate 1,2-dioxygenase.’ Biology and Fertility of Soils 23: 307-313.
  • Rosche B, Tshisuaka B, Fetzner S, Lingens F. . ‘2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudomonas putida 8.’ Journal of Biological Chemistry 270: 17836-17842.
  • Rosche B, Fetzner S, Lingens F, Nitschke W, Riedel A. . ‘The 2Fe2S centres of the 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy.’ Biochimica et Biophysica Acta 1252: 177-179.
  • Haak B, Fetzner S, Lingens F. . ‘Cloning, nucleotide sequence, and expression of the plasmid-encoded genes for the two-component 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS.’ Journal of Bacteriology 177: 667-675.
  • Riedel A, Fetzner S, Lingens F, Liebl U, Zimmermann J-L, Nitschke W. . ‘EPR, Electron Spin Echo Envelope Modulation, and Electron Nuclear Double Resonance studies of the 2Fe2S centres of the 2-halobenzoate 1,2-dioxygenase from Burkholderia (Pseudomonas) cepacia 2CBS.’ Journal of Biological Chemistry 270: 30869-30873.
  • Schach S, Tshisuaka B, Fetzner S, Lingens F. . ‘Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63: The first two enzymes in quinoline and 3-methylquinoline degradation.’ European Journal of Biochemistry 232: 536-544.
  • Lehmann M, Tshisuaka B, Fetzner S, Lingens F. . ‘Molecular cloning of the iso-quinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of IorA and IorB, and sequence comparisons with other molybdenum-containing hydroxylases.’ Journal of Biological Chemistry 270: 14420-14429.
  • Fetzner S, Lingens F. . ‘Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications.’ Microbiological Reviews 58: 641-685.
  • Sauter M, Tshisuaka B, Fetzner S, Lingens F. . ‘Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases.’ Journal of Biological Chemistry 374: 1037-1046.
  • Lehmann M, Tshisuaka B, Fetzner S, Röger P, Lingens F. . ‘Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase.’ Journal of Biological Chemistry 269: 11254-11260.
  • Bauer I, de Beyer A, Tshisuaka B, Fetzner S, Lingens F. . ‘A novel type of oxy-genolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline.’ FEMS Microbiology Letters 117: 299-304.
  • Schach S, Schwarz G, Fetzner S, Lingens F. . ‘Microbial metabolism of quinoline and related compounds. XVII. Degradation of 3-methylquinoline by Comamonas testosteroni 63.’ Biological Chemistry Hoppe-Seyler 374: 175-181.
  • Fetzner S, Lingens F. . ‘Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1.’ Biological Chemistry Hoppe-Seyler 374: 363-376.
  • Fetzner S, Vogler B, Lingens F. . ‘Transformation of 2-chloroquinoline to 2-chloro-cis-7,8-dihydro-7,8-dihydroxyquinoline by quinoline-grown resting cells of Pseudomonas putida 86.’ FEMS Microbiology Letters 112: 151-158.
  • Fetzner S, Müller R, Lingens F. . ‘Purification and some properties of 2-halo-benzoate 1,2-dioxygenase, a two-component enzyme system from Pseudomonas cepacia 2CBS.’ Journal of Bacteriology 174: 279-290.
  • Fetzner S, Müller R, Lingens F. . ‘Degradation of 2-chlorobenzoate by Pseudomonas cepacia 2CBS.’ Biological Chemistry Hoppe-Seyler 370: 1173-1182.
  • Fetzner S, Müller R, Lingens F. . ‘A novel metabolite in the microbial degradation of 2-chlorobenzoate.’ Biochemical Biophysical Research Communications 161: 700-705.