Dekanin des Fachbereichs Biologie

Prof. Dr. Susanne Fetzner
© Uni MS

Fetzner, Susanne, Prof. Dr. rer. nat.
Westfälische Wilhelms-Universität Münster
Institut für Molekulare Mikrobiologie und Biotechnologie (IMMB)
Corrensstraße 3
D-48149 Münster

Tel. +49 (0)251 / 83-2 30 12
dekanat.bio@uni-muenster.de

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

  • Allgemeine Mikrobiologie
  • Mikrobieller Stoffwechsel, Biodegradation
  • Enzymbiochemie

Forschungsschwerpunkte

  • Biochemie bakterieller Stoffwechselwege
  • Mechanismen enzymkatalysierter Reaktionen

Ausgewählte Projekte

  • Alkylquinolone biosynthesis in Pseudomonas aeruginosa
  • Inactivation of Pseudomonas aeruginosa alkylquinolone-type quorum sensing signals and antibiotics
  • Cofactor-less dioxygenases to interfere with quorum sensing signaling and virulence of Pseudomonas aeruginosa

Ausgewählte Publikationen

  • Wullich SC, Kobus S, Wienhold M, Hennecke U, Smits SHJ, Fetzner S (2019) Structural basis for recognition and ring-cleavage of the Pseudomonas quinolone signal (PQS) by AqdC, a mycobacterial dioxygenase of the α/β-hydrolase fold family. J Struct Biol. 207: 287-294.
  • Thierbach S, Birmes FS, Letzel MC, Hennecke U, Fetzner S (2017) Chemical modification and detoxification of the Pseudomonas aeruginosa toxin 2-heptyl-4-hydroxyquinoline N-oxide by environmental and pathogenic bacteria. ACS Chem. Biol. 12: 2305-2312.
  • Drees SL, Li C, Prasetya F, Saleem M, Dreveny I, Williams P, Hennecke U, Emsley J, Fetzner S (2016) PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: Crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291: 6610-6624.
  • Drees SL, Fetzner S (2015) PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22: 611-618.
  • Thierbach S, Bui N, Zapp J, Chhabra SR, Kappl R, Fetzner S (2014) Substrate-assisted O2 activation in a cofactor-independent dioxygenase. Chem. Biol. 21: 217-225.
  • Steiner RA, Janßen HJ, Roversi P, Oakley AJ, Fetzner S (2010) Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the α/β hydrolase fold. Proc. Natl. Acad. Sci. USA 107: 657-662.

Ausgewählte Übersichtsartikel/Sonderbeiträge:

  • Fetzner S (2015) Quorum quenching enzymes. J. Biotechnol. 201: 2-11.
  • Fetzner S, Drees SL (2013) Old molecules, new biochemistry. Chem. Biol. 20: 1438-1440.
  • Fetzner S (2007) Cofactor-independent oxygenases go it alone. Nat. Chem. Biol. 3: 374-375.

Publikationen

  • Arranz San Martín A, Vogel J, Wullich SC, Quax WJ, Fetzner S. . ‘Enzyme-Mediated Quenching of the Pseudomonas Quinolone Signal (PQS): A Comparison between Naturally Occurring and Engineered PQS-Cleaving Dioxygenases.’ Biomolecules 12: 170. doi: 10.3390/biom12020170.
  • Ernst, S; Mährlein, A; Ritzmann, NH; Drees, SL; Fetzner, S. . ‘A comparative study of N-hydroxylating flavoprotein monooxygenases reveals differences in kinetics and cofactor binding.’ The FEBS Journal 289, Nr. 18: 5637–5655. doi: doi: 10.1111/febs.16444.
  • Ernst, S; Volkov, AN; Stark, M; Hölscher, L; Steinert, K; Fetzner, S; Hennecke, U; Drees, SL. . ‘Azetidomonamide and Diazetidomonapyridone metabolites control biofilm formation and pigment synthesis in Pseudomonas aeruginosa.’ Journal of the American Chemical Society 144, Nr. 17: 7676–7685. doi: doi: 10.1021/jacs.1c13653.
  • Arranz San Martín, A; Drees, SL; Fetzner, S. . ‘A PQS-Cleaving Quorum Quenching Enzyme Targets Extracellular Membrane Vesicles of Pseudomonas aeruginosa.’ Biomolecules 12, Nr. 11: 1656. doi: DOI: 10.3390/biom12111656.
  • Sartor P, Denkhaus L, Gerhardt S, Einsle O, Fetzner S. . ‘Structural basis of O-methylation of (2-heptyl-)1-hydroxyquinolin-4(1H)-one and related compounds by the heterocyclic toxin methyltransferase Rv0560c of Mycobacterium tuberculosis.’ Journal of Structural Biology 213(4):107794. doi: 10.1016/j.jsb.2021.107794.
  • Panasia G, Drees SL, Fetzner S, Philipp B. . ‘A Complex of LaoA and LaoB Acts as a Tat-Dependent Dehydrogenase for Long-Chain Alcohols in Pseudomonas aeruginosa.’ Applied and Environmental Microbiology 87(16):e0076221. doi: 10.1128/AEM.00762-21.
  • Ritzmann NH, Drees SL, Fetzner S. . ‘Signal synthase-type versus catabolic monooxygenases: Retracing 3-hydroxylation of 2-alkylquinolones and their N-oxides by Pseudomonas aeruginosa and other pulmonary pathogens.’ Applied and Environmental Microbiology 87. doi: 10.1128/AEM.02241-20.
  • Wullich SC, Wijma HJ, Janssen DB, Fetzner S. . ‘Stabilizing AqdC, a Pseudomonas Quinolone Signal-Cleaving Dioxygenase from Mycobacteria, by FRESCO-based Protein Engineering.’ ChemBioChem 22.
  • Sartor P, Bock J, Hennecke U, Thierbach S, Fetzner S. . ‘Modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4(1H)-one and other secondary metabolites by methyltransferases from mycobacteria.’ The FEBS Journal 288. doi: 10.1111/febs.15595.
  • Ernst S, Rovida S, Mattevi A, Fetzner S, Drees SL. . ‘Photoinduced monooxygenation involving NAD(P)H-FAD sequential single-electron transfer.’ Nature Communications 11. doi: 10.1038/s41467-020-16450-y.
  • Wullich SC, Arranz San Martin A, Fetzner S. . ‘Definition of an α/β-hydrolase fold subfamily comprising Pseudomonas quinolone signal cleaving dioxygenases.’ Applied and Environmental Microbiology 86. doi: 10.1128/AEM.00279-20.
  • Rieger B, Thierbach S, Ommer M, Dienhart FSV, Fetzner S, Busch KB. . ‘Pseudomonas Quinolone Signal molecule PQS behaves as a B Class like inhibitor at the IQ site of mitochondrial complex I.’ FASEB BioAdvances 2. doi: 10.1096/fba.2019-00084.
  • Thierbach S, Sartor P, Yücel O, Fetzner S. . ‘Efficient modification of the Pseudomonas aeruinosa toxin 2-heptyl-1-hydroxyquinolin-4-one by three Bacillus glycosyltransferases with broad substrate ranges.’ J. Biotechnol. 308. doi: 10.1016/j.jbiotec.2019.
  • Birmes FS, Säring R, Hauke MC, Ritzmann NH, Drees SL, Daniel J, Treffon J, Liebau E, Kahl B, Fetzner S. . ‘Interference with Pseudomonas aeruginosa quorum sensing and virulence by the mycobacterial PQS dioxygenase AqdC in combination with the N-acylhomoserine lactone lactonase QsdA.’ Infect. Immun. 87. doi: 10.1128/IAI.00278-19.
  • Wullich SC, Kobus S, Wienhold M, Hennecke U, Smits SHJ, Fetzner S. . ‘Structural basis for recognition and ring-cleavage of the Pseudomonas quinolone signal (PQS) by AqdC, a mycobacterial dioxygenase of the α/β-hydrolase fold family.’ J. Struct. Biol. 207. doi: 10.1016/j.jsb.2019.06.006.
  • Ritzmann NH, Mährlein A, Ernst S, Hennecke U, Drees SL, Fetzner S. . ‘Bromination of alkyl quinolones by Microbulbifer sp. HZ11, a marine Gammaproteobacterium, modulates their antibacterial activity.’ Environ. Microbiol. 21. doi: 10.1111/1462-2920.14654.
  • Thierbach S, Wienhold M, Fetzner S, Hennecke U. . ‘Synthesis and biological activity of methylated derivatives of the Pseudomonas metabolites HHQ, HQNO und PQS.’ Beilstein J. Org. Chem. 15. doi: 10.3762/bjoc.15.18.
  • Drees SL, Ernst S, Belviso BD, Jagmann N, Hennecke U, Fetzner S. . ‘PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa.’ J. Biol. Chem. 293, Nr. 24. doi: 10.1074/jbc.RA117.000789.
  • Thierbach S, Birmes FS, Letzel MC, Hennecke U, Fetzner S. . ‘Chemical modification and detoxification of the Pseudomonas aeruginosa toxin 2-heptyl-4-hydroxyquinoline N-oxide by environmental and pathogenic bacteria.’ ACS Chemical Biology 12. doi: 10.1021/acschembio.7b00345.
  • Maura D, Drees SL, Bandyopadhaya A, Kitao T, Negri M, Starkey M, Lesic B, Milot S, Déziel E, Zahler R, Pucci M, Felici A, Fetzner S, Lépine F, Rahme LG. . ‘Polypharmacology approaches against the Pseudomonas aeruginosa MvfR regulon and their application in blocking virulence and antibiotic tolerance.’ ACS Chem. Biol. 12. doi: 10.1021/acschembio.6b01139.
  • Birmes FS, Wolf T, Kohl TA, Rüger K, Bange F, Kalinowski J, Fetzner S. . ‘Mycobacterium abscessus subsp. abscessus is capable of degrading Pseudomonas aeruginosa quinolone signals.’ Front. Microbiol. 8. doi: 10.3389/fmicb.2017.00339.
  • 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 Chemistry Jan 25, 2016.
  • 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, Nr. 10: 3281–3284. doi: 10.1002/anie.201510741.
  • 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, Nr. 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, Nr. 6: 1755–1763. doi: 10.1021/acschembio.6b00156.
  • Birmes F., Fetzner S. . „Bakterielle Kommunikation: Signale und Signal-inaktivierende Enzyme.“ BIOspektrum 22, Nr. 3: 251–254. doi: 10.1007/s12268-016-0681-4.
  • Drees S., Fetzner S. . ‘PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules.’ Chemistry and Biology 22, Nr. 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, Nr. 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, Nr. null. doi: 10.1111/1462-2920.12857. [online first]
  • 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, Nr. 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, Nr. null: 99–100. doi: 10.1016/j.jbiotec.2015.07.014.
  • 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, Nr. 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, Nr. 23: 7266–7274. doi: 10.1128/AEM.02342-14.
  • 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.
  • 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, Nr. 5: 1068–1080. doi: 10.1128/JB.01547-12.
  • Fetzner S., Drees S.L. . ‘Old molecules, new biochemistry.’ Chemistry and Biology 20, Nr. 12: 1438–1440. doi: 10.1016/j.chembiol.2013.12.001.
  • Niewerth H, Schuldes J, Parschat K, Kiefer P, Vorholt JA, Daniel R, Fetzner S. . ‘Complete genome sequence and metabolic potential of the quinaldine-degrading bacterium Arthrobacter sp. Rue61a.’ BMC Genomics 13, Nr. 1: 534. doi: 10.1186/1471-2164-13-534.
  • Müller C, Fetzner S. . ‘A Pseudomonas putida bioreporter for the detection of enzymes active on 2-alkyl-4(1H)-quinolone signalling molecules.’ Applied Microbiology and Biotechnology to be assigned. doi: 10.1007/s00253-012-4236-4.
  • Fetzner S. . ‘Ring-cleaving dioxygenases with a cupin fold.’ Applied and Environmental Microbiology 78, Nr. 8: 2505. doi: 10.1128/AEM.07651-11.
  • Thierbach S, Büldt-Karentzopoulos K, Dreiling A, Hennecke U, König S, Fetzner S. . ‘Hydrolase-like properties of a cofactor-independent dioxygenase.’ ChemBioChem 13, Nr. 8: 1125–7. doi: 10.1002/cbic.201200152.
  • Niewerth H, Bergander K, Chhabra SR, Williams P, Fetzner S. . ‘Synthesis and biotransformation of 2-alkyl-4(1H)-quinolones by recombinant Pseudomonas putida KT2440.’ Applied Microbiology and Biotechnology 91, Nr. 5: 1399. doi: 10.1007/s00253-011-3378-0.
  • Kolkenbrock S, Naumann B, Hippler M, Fetzner S. . ‘A Novel Replicative Enzyme Encoded by the Linear Arthrobacter Plasmid pAL1.’ Journal of Bacteriology 192, Nr. 19: 4935–4943. doi: 10.1128/JB.00614-10.
  • Fetzner S, Steiner RA. . ‘Cofactor-independent oxidases and oxygenases.’ Applied Microbiology and Biotechnology 86, Nr. 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, Nr. 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 America (PNAS) 107, Nr. 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, 865-886. Springer VDI Verlag. 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 and Biology 16, Nr. 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, Nr. 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, Nr. 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, Nr. 27: 7116–7126. doi: 10.1021/bi800554v.
  • Fetzner S. . ‘Cofactor-independent oxygenases go it alone.’ Nature Chemical Biology 3, Nr. 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, Nr. 6: 475–487. doi: 10.1007/s00203-007-0215-z.
  • 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, Nr. 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 Communications 63: 378–381. doi: 10.1107/S1744309107013760.
  • 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 Communications 63: 382–385. doi: 10.1107/S174430910701353X.
  • 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.
  • 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, Nr. 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, Nr. 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, 63–98. Springer VDI Verlag.
  • 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, Nr. 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, Nr. 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, Nr. 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, Nr. 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, Nr. 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, Nr. 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 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 Communications 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, Nr. 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, Nr. 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, Nr. 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, Nr. 7: 1567–1577. doi: 10.1046/j.1432-1033.2003.03526.x.
  • Berthe-Corti L, Fetzner S. . ‘Bacterial metabolism of n-alkanes and ammonia under oxic, suboxic and anoxic conditions.’ Acta Biotechnologica 22, Nr. 3-4: 299–336. doi: 10.1002/1521-3846(200207)22:3/4299::AID-ABIO299>3.0.CO;2-F.
  • Andreesen JR, Fetzner S. . ‘The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine.’, 405–430.
  • Kappl R, Huttermann J, Fetzner S. . ‘The molybdenum-containing hydroxylases of quinoline, isoquinoline, and quinaldine.’, 481–537.
  • Fetzner S. . ‘Oxygenases without requirement for cofactors or metal ions.’ Applied Microbiology and Biotechnology 60, Nr. 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, Nr. 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. 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, Nr. 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, Nr. 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, Nr. 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.
  • 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. . ‘Bioconversion of pyrimidine by resting cells of quinoline-degrading bacteria.’ FEMS Microbiology Letters 176: 291–299.
  • 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.
  • 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.
  • Fetzner S. . ‘Bacterial dehalogenation.’ Applied Microbiology and Biotechnology 50: 633–657.
  • 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: 577.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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, 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.
  • 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, 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.