• Original-Veröffentlichungen (seit 1999)


    88. Ritzmann NH, Drees SL, Fetzner S (2021) Signal synthase-type versus catabolic monooxygenases: Retracting 3-hydroxylation of 2-alkylquinolones and their N-oxides by Pseudomonas aeruginosa and other pulmonary pathogens.
    Appl Environ Microbiol. 2021 Jan 15:AEM.02241-20. Online ahead of print. Doi: 10.1128/AEM.02241-20


    87. Wullich SC, Wijma HJ, Janssen DB, Fetzner S (2020) Stabilizing AqdC, a Pseudomonas Quinolone Signal-Cleaving Dioxygenase from Mycobacteria, by FRESCO-based Protein Engineering.
    ChemBioChem. 2020 Oct 14. doi: 10.1002/cbic.202000641. Online ahead of print.

    86. Sartor P, Bock J, Hennecke U, Thierbach S, Fetzner S (2020) Modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4(1H)-one and other secondary metabolites by methyltransferases from mycobacteria.
    FEBS J. 2020 Oct 16.Doi:10.1111/febs.15595. Online ahead of print.

    85. Ernst S, Rovida S, Mattevi A, Fetzner S, Drees SL (2020) Photoinduced monooxygenation involving NAD(P)H-FAD sequential single-electron transfer.  Nat. Commun. 11:2600.

    84. Wullich SC, Arranz San Martin A, Fetzner S (2020) Definition of an α/β-hydrolase fold subfamily comprising Pseudomonas quinolone signal cleaving dioxygenases.
    Appl. Environ. Microbiol. 86(9): e00279-20. doi: 10.1128/AEM.00279-20.
    83. Rieger B, Thierbach S, Ommer M, Dienhart FSV, Fetzner S, Busch KB (2020) Pseudomonas Quinolone Signal molecule PQS behaves as a B Class like inhibitor at the IQ site of mitochondrial complex I.
    FASEB bioadv. 2(3):188-202. doi: 10.1096/fba.2019-00084. eCollection 2020 Mar.

    82. Thierbach S, Sartor P, Yücel O, Fetzner S (2020) Efficient modification of the Pseudomonas aeruinosa toxin 2-heptyl-1-hydroxyquinolin-4-one by three Bacillus glycosyltransferases with broad substrate ranges. J. Biotechnol. 308:74-81. doi: 10.1016/j.jbiotec.2019.11.015. Epub 2019 Nov 28.


    81. Birmes FS, Säring R, Hauke MC, Ritzmann NH, Drees SL, Daniel J, Treffon J, Liebau E, Kahl B, Fetzner S (2019) 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(10). pii: e00278-19. doi: 10.1128/IAI.00278-19. Print 2091 Oct.

    80. 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. doi: 10.1016/j.jsb.2019.06.006. Epub 2019 Jun 19.

    79. Ritzmann NH, Mährlein A, Ernst S, Hennecke U, Drees SL, Fetzner S (2019) Bromination of alkyl quinolones by Microbulbifer sp. HZ11, a marine Gammaproteobacterium, modulates their antibacterial activity.
    Environ Microbiol. 21:2595-2609. doi: 10.1111/1462-2920. 14654. Epub 2019 Jun 6.

    78. Thierbach S, Wienhold M, Fetzner S, Hennecke U (2019) Synthesis and biological activity of methylated derivatives of the Pseudomonas metabolites HHQ, HQNO und PQS.
    Beilstein J Org.Chem. 15:187-184. doi: 10.3762/bjpoc.15.18. eCollection 2019.


    77. Drees SL, Ernst S, Belviso BD, Jagmann N, Hennecke U, Fetzner S (2018) PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa.
     J. Biol Chem.2018 jun 15; 293(24):9345-9357. doi: 10.1074/jbc.RA117.000789. Epub 2018 Apr 18.


    76. 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. doi: 10.1021/acschembio.7b00345.

    75. 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 (2017) Polypharmacology approaches against the Pseudomonas aeruginosa MvfR regulon and their application in blocking virulence and antibiotic tolerance.
     ACS Chem. Biol. 12: 1435-1443. doi: 10.1021/acschembio.6b01139. Epub 2017 Apr 12.

    74. Birmes FS, Wolf T, Kohl TA, Rüger K, Bange F, Kalinowski J, Fetzner S (2017) Mycobacterium abscessus subsp. abscessus is capable of degrading Pseudomonas aeruginosa quinolone signals.
    Front Microbiol. 8:339. doi: 10.3389/fmicb.2017.00339.


    73. Tettmann B, Niewerth C, Kirschhöfer F, Neidig A, Dötsch A, Brenner-Weiss G, Fetzner S, Overhage J (2016) Enzyme-mediated quenching of the Pseudomonas quinolone signal (PQS) promotes biofilm formation of Pseudomonas aeruginosa by increasing iron availability. Front. Microbiol. 7:1978. doi: 10.3389/fmicb.2016.01978

    72. Zender M, Witzgall F, Drees SL, Weidel E, Maurer CK, Fetzner S, Blankenfeldt W, Empting M, Hartmann RW (2016) Dissecting the multiple roles of PqsE in Pseudomonas aeruginosa virulence by discovery of small tool compounds. 
     ACS Chem Biol. 11: 1755-1763. doi: 10.1021/acschembio.6b00156.

    71. Jeoung J-H, Nianios D, Fetzner S, Dobbek H (2016) Quercetin 2,4-dioxygenase activates dioxygen in a side-on O2-Ni complex. Angew. Chem. Int. Ed. 55: 3281-3284.

    70. 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. doi: 10.1074/jbc.M115.708453.


    69. Müller C, Birmes FS, Rückert C, Kalinowski J, Fetzner S (2015) Rhodococcus erythropolis BG43 genes mediating Pseudomonas aeruginosa quinolone signal degradation and virulence  factor attenuation.
     Appl. Environ. Microbiol. 81: 7720-7729.

    68. Rückert C, Birmes FS, Müller C, Niewerth H, Winkler A, Fetzner S, Kalinowski J (2015) Complete genome sequence of Rhodococcus erythropolis BG43 (DSM 46869), a degrader of Pseudomonas aeruginosa quorum sensing signal molecules.
    J. Biotechnol. 211: 99-100.

    67. 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.

    66. Nianios D, Thierbach S, Steimer L, Lulchev P, Klostermeier D, Fetzner S (2015) Nickel quercetinase, a "promiscuous" metalloenzyme: Metal incorporation and metal ligand substitution studies.
    BMC Biochemistry 16:10. DOI:10.1186/s12858-015-0039-4

    65. Soh EY, Chhabra SR, Halliday N, Heeb S, Müller C, Birmes FS, Fetzner S, Cámara M, Chan KG, Williams P (2015)
    Biotic inactivation of the Pseudomonas aeruginosa quorum sensing signal molecule PQS
    Environ. Microbiol. 17: 4352-4365. doi: 10.1111/1462-2920.


    64. Müller C, Birmes FS, Niewerth H, Fetzner S (2014) Conversion of the Pseudomonas aeruginosa quinolone signal (PQS) and related alkylhydroxyquinolines by Rhodococcus sp. strain BG43.
    Appl. Environ. Microbiol. 80: 7266-7274.

    63. Wagner UG, DiMaio F, Kolkenbrock S, Fetzner S (2014) Crystal structure analysis of EstA from Arthrobacter sp. Rue61a - an insight into catalytic promiscuity.
    FEBS Lett. 588: 1154-1160.

    62. 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.
    Referred to by: Bugg, T.D.H.: How to break the rules of dioxygen activation.
    Chem. & Biol. 21: 168-169 ("Preview")


    61. Niewerth H, Parschat K, Rauschenberg M, Ravoo BJ, Fetzner S (2013) The PaaX-type repressor MeqR2 of Arthrobacter sp. Rue61a involved in regulation of quinaldine catabolism binds to its own and to catabolic promoters and specifically responds to anthraniloyl-CoA.
    J. Bacteriol. 195: 1068-1080.

    60. Müller C, Fetzner S (2013) A Pseudomonas putida bioreporter for the detection of enzymes active on 2-alkyl-4(1H)-quinolone signalling molecules.
    Appl. Microbiol. Biotechnol. 97: 751-760.


    59. Niewerth H, Schuldes J, Parschat K, Kiefer P, Vorholt JA, Daniel R, Fetzner S (2012) Complete genome sequence and metabolic potential of the quinaldine-degrading bacterium Arthrobacter sp. Rue61a.
    BMC Genomics 2012, 13:534. DOI: 10.1186/1471-2164-13-534

    58. Thierbach S, Büldt-Karentzopoulos K, Dreiling A, Hennecke U, König S, Fetzner S (2012) Hydrolase-like properties of a cofactor-independent dioxygenase. ChemBioChem 13: 1125-1127.


    57. Niewerth H, Bergander K, Chhabra SR, Williams P, Fetzner S (2011) Synthesis and biotransformation of 2-alkyl-4(1H)-quinolones by recombinant Pseudomonas putida KT2440.
    Appl. Microbiol. Biotechnol. 91: 1399-1408


    56. Kolkenbrock S, Naumann B, Hippler M, Fetzner S (2010) A novel replicative enzyme encoded by the linear Arthrobacter plasmid pAL1.
    J. Bacteriol. 192: 4935-4943.

    55. Kolkenbrock S, Fetzner S (2010) Identification and in vitro deoxynucleotidylation of the terminal protein of the linear plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a.
    FEMS Microbiol. Lett. 304: 169-176.

    54. 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.


    53. Pustelny C, Albers A, Büldt-Karentzopoulos, K, Parschat K, Chhabra SR, Camara M, Williams P, Fetzner S (2009) Dioxygenase-mediated quenching of quinolone-dependent quorum sensing in Pseudomonas aeruginosa.
    Chem. & Biol. 16: 1259-1267.


    52. Merkens H, Kappl R, Jakob RP, Schmid FX, Fetzner S (2008) Quercetinase QueD of Streptomyces sp. FLA, a monocupin dioxygenase with a preference for nickel and cobalt.
    Biochemistry 47: 12185-12196.

    51. Merkens H, Fetzner S (2008) Transcriptional analysis of the queD gene coding for quercetinase of Streptomyces sp. FLA.
    FEMS Microbiol. Lett. 287: 100-107.

    50. Boehm K, Guddorf J, Albers A, Kamiyama T, Fetzner S, Hinz H-J (2008) Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism.
    Biochemistry 47: 7116-7126.


    49. Steiner RA, Frerichs-Deeken U, Fetzner S (2007) Crystallization and preliminary X-ray analysis of 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the α/β hydrolase fold superfamily.
    Acta Cryst. F63: 382-385.

    48. Qi R, Fetzner S, Oakley AJ (2007) Crystallization and diffraction data of 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β hydrolase family.
    Acta Cryst. F63: 378-381.

    47. Parschat K, Overhage J, Henne A, Strittmatter AW, Gottschalk G, Fetzner S (2007) Complete nucleotide sequence of the 113 kb linear catabolic plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a, and transcriptional analysis of genes involved in quinaldine degradation.
    J. Bacteriol. 189: 3855-3867.

    46. Beermann B, Guddorf J, Böhm K, Albers A, Kolkenbrock S, Fetzner S, Hinz H-J (2007) Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase.
    Biochemistry 46: 4241-4249.

    45. Merkens H, Sielker S, Rose K, Fetzner S (2007) 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.
    Arch. Microbiol. 187: 475-487.

    44. Schütte M, Fetzner S (2007) EstA from Arthrobacter nitroguajacolicus Rü61a, a thermo- and solvent-tolerant carboxylesterase related to class C ß-lactamases.
    Curr. Microbiol. 54: 230-236.


    43. Kolkenbrock S, Parschat K, Beermann B, Hinz H-J, Fetzner S (2006) N-Acetylanthranilate amidase from Arthrobacter nitroguajacolicus Rü61a, an α/β-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant.
    J. Bacteriol. 188:8430-8440.
    Erratum in: J. Bacteriol. 189: 3933 (2007).

    42. Kappl R, Sielker S, Ranguelova K, Wegner J, Parschat K, Hüttermann J, Fetzner S (2006) Spectroscopic and biochemical studies on protein variants of quinaldine 4-oxidase: role of E736 in catalysis and effects of serine ligands to the FeSI and FeSII clusters.
    Biochemistry 45: 14853-14868.

    41. Rose K, Fetzner S (2006) Identification of linear plasmid pAM1 in the flavonoid degrading strain Actinoplanes missouriensis (DSM 43046).
    Plasmid 55: 249-254.


    40. Carl B, Fetzner S (2005) 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.
    Appl. Environ. Microbiol. 71: 8618-8626.

    39. Frerichs-Deeken U, Fetzner S (2005) 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.
    Curr. Microbiol. 51: 344-352.

    38. Purvanov V, Fetzner S (2005) Replacement of active-site residues of quinoline 2-oxidoreductase involved in substrate recognition and specificity.
    Curr. Microbiol. 50: 217-222.

    37. Overhage J, Sielker S, Homburg S, Parschat K, Fetzner S (2005) Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate.
    Microbiology 151: 491-500.

    36. Boer DR, Müller A, Fetzner S, Lowe DJ, Romão MJ (2005) On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7.
    Acta Cryst. F61: 137-140.


    35. Frerichs-Deeken U, Ranguelova K, Kappl R, Hüttermann J, Fetzner S (2004) 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: 14485-14499.

    34. Bonin I, Martins BM, Purvanov P, Fetzner S, Huber R, Dobbek H (2004) Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.
    Structure 12: 1425-1435.

    33. Carl B, Arnold A, Hauer B, Fetzner S (2004) Sequence and transcriptional analysis of a gene cluster of Pseudomonas putida 86 involved in quinoline degradation.
    Gene 331: 177-188.


    32. Parschat K, Hauer B, Kappl R, Kraft R, Hüttermann J, Fetzner S (2003) Gene cluster of Arthrobacter ilicis Rü61a involved in the degradation of quinaldine to anthranilate: Characterization and functional expression of the quinaldine 4-oxidase qoxLMS genes.
    J Biol Chem 278: 27483-27494.

    31. Frerichs-Deeken U, Goldenstedt B, Gahl-Janßen R, Kappl R, Hüttermann J, Fetzner S (2003) Functional expression of the quinoline 2-oxidoreductase genes (qorMSL) in Pseudomonas putida KT2440 pUF1 and in Pseudomonas putida 86-1 Δqor pUF1 and analysis of the Qor proteins.
    Eur. J. Biochem. 270: 1567-1577.


    30. Israel I., Sohni M., Fetzner S. (2002) Expression of the iorAB genes from Brevundimonas diminuta 7 encoding the molybdenum hydroxylase isoquinoline 1-oxidoreductase in Pseudomonas putida.
    FEMS Microbiol. Lett. 210: 123-127.


    29. Parschat K., Canne C., Kappl R., Hüttermann J., Fetzner S. (2001) Xanthine dehydrogenase from Pseudomonas putida 86: Specificity, oxidation-reduction potentials of its redox-active centers, and first EPR studies.
    Biochim. Biophys. Acta 1544: 151-165.


    28. Fischer F., Fetzner S. (2000) 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 Microbiol. Lett. 190: 21-27.


    27. Fischer F., Künne S., Fetzner S. (1999) Bacterial 2,4-dioxygenases: New members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.
    J. Bacteriol. 181: 5725-5733.

    26. Canne C., Lowe D.J., Fetzner S., Adams B., Smith A.T., Kappl R., Bray R.C., Hüttermann J. (1999) Kinetics and interactions of molybdenum and iron-sulfur centres in bacterial enzymes of the xanthine oxidase family: Mechanistic implications.
    Biochemistry 38: 14077-14087.

    25. Fetzner S. (1999) Bioconversion of pyrimidine by resting cells of quinoline-degrading bacteria.
    FEMS Microbiol. Lett. 176: 291-299.

    24. Hund H. K., Breuer J., Lingens F., Hüttermann J., Kappl R., Fetzner S. (1999) Flavonol 2,4-dioxygenase from Aspergillus niger DSM 821, a type 2 CuII–containing glycoprotein.
    Eur. J. Biochem. 263: 871-878.

    23. Max N., Betz A., Facey S., Lingens F., Hauer B., Fetzner S. (1999) 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.
    Biochim. Biophys. Acta 1431: 547-552.

  • Reviews und Sonderartikel

    18. Birmes FS, Fetzner S (2016) Bakterielle Kommunikation: Signale und Signal-inaktivierende Enzyme.
    BIOspektrum 22: 251-254.

    17. Fetzner S (2015) Quorum quenching enzymes
    J Biotechnol. 201: 2-11

    16. Fetzner S, Drees SL (2013) Old molecules, new biochemistry.
    Chem. & Biol.20: 1438-1440

    15. Fetzner S (2012) Ring-cleaving dioxygenases with a cupin fold.
      Appl. Environ. Microbiol. 78: 2505-2514.
    14. Fetzner, S, Steiner RA (2010) Cofactor-independent oxidases and oxygenases.
    Appl. Microbiol. Biotechnol. 86: 791-804.

    13. Fetzner, S (2010) Aerobic Degradation of Halogenated Aliphatics.
    In: Handbook of Hydrocarbon and Lipid Microbiology, Part 10, Biochemistry of Aerobic Degradation, pp 865-885 (edited by K. N. Timmis). Springer, Berlin, Heidelberg 2010.

    12. Fetzner S (2007) Cofactor-independent oxygenases go it alone.
    Nature Chem. Biol. 3: 374-375.

    11. Fetzner S, Kolkenbrock S, Parschat K (2007) Catabolic linear plasmids.
    In: Meinhardt F, Klassen R (eds.) Microbiology Monographs, vol 7: Microbial linear plasmids, pp 63-98. Springer-Verlag, Berlin Heidelberg 2007.

    10. Fetzner S. (2002) Oxygenases without requirement for cofactors or metal ions.
     Appl. Microbiol. Biotechnol. 60: 243-257.

    9. Kappl R., Hüttermann J., Fetzner S. (2002) The molybdenum-containing hydroxylases of quinoline, isoquinoline, and quinaldine.
    In: Molybdenum and Tungsten. Their Roles in Biological Processes. Vol. 39 of Met. Ions Biol. Syst. (A. Sigel, H. Sigel, Eds.), pp 481-538, Marcel Dekker, New York.

    8. Andreesen J.R., Fetzner S. (2002) The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine.
    In: Molybdenum and Tungsten. Their Roles in Biological Processes. Vol. 39 of Met. Ions Biol. Syst. (A. Sigel, H. Sigel, Eds.), pp 405-430, Marcel Dekker, New York.

    7. Fetzner, S. (2002): Biodegradation of Xenobiotics. In: Doelle & Da Silva (Eds.): Biotechnology. In: Encyclopedia of Life Support Systems (EOLSS), developed under the Auspices of the UNESCO, Eolss Publishers, Oxford, UK

    6. Berthe-Corti L., Fetzner S. (2002) Bacterial metabolism of alkanes and ammonia under oxygen depleted conditions.
    Acta Biotechnol. 22: 299-336.

    5. Fetzner S. (2000) Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: Molybdenum hydroxylases and ring-opening 2,4-dioxygenases.
    Naturwissenschaften 87: 59-69.

    4. Fetzner S. (1998) Bacterial dehalogenation.
    Appl. Microbiol. Biotechnol. 50: 633 - 657.

    3. Fetzner S. (1998) Bacterial degradation of pyridine, indole, quinoline, and their derivatives under different redox conditions.
    Appl. Microbiol. Biotechnol. 49: 237 - 250.

    2. Fetzner S, Tshisuaka B, Lingens F, Kappl R, Hüttermann J (1998) Bacterial degradation of quinoline and -derivatives - pathways and their biocatalysts.
    Angew. Chem. Int. Ed. 37: 576 - 597.

    1. Fetzner S, Lingens F (1994) Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications.
    Microbiol. Rev. 58: 641 - 685.