Quinoline oxidoreductase

Bauder R, B Tshisuaka, F Lingens (1990) Microbial metabolism of quinoline and related compounds VII. Quinoline oxidoreductase from Pseudomonas putida a molybdenum-containing enzyme. Biol Chem Hoppe-Seyler 371 1137-1144. 

Peschke, B., and Lingens, F., Microbial Metabohsm of Quinohne and Related Compounds. XII. Isolation and Characterization of the Quinohne Oxidoreductase From Rhodococcus Spec. B1 Compared With the Quinoline Oxidoreductase From Pseudomonas Putida 86. Biol. Chem. Hoppe-Seyler, 1991. 372 pp. 1081-1088. 

Tshisuaka, B. Kappl, R. Huttermann, J., and Lingens, F., Quinoline Oxidoreductase From Pseudomonas-Putida-86 - an Improved Purification Procedure and Electron-Paramagnetic-Resonance Spectroscopy. Biochemistry-US, 1993. 32 (47) pp. 12928-12934. 

Fe2S2] clusters are part of the molybdenum containing hydroxylases. Typically, apart from molybdenum and two EPR-distinct iron-sulfur centres there can be FAD as additional cofactor. In Chlostridium purinolyticum a selenium-dependent purine hydroxylase has been characterized as molybdenum hydroxylase. The EPR of the respective desulfo molybdenum (V) signal indicated that the Mo-ligands should differ from those of the well known mammalian corollary xanthine oxidase.197 For the bacterial molybdenum hydroxylase quinoline oxidoreductase from Pseudomonas putida an expression system was developed in order to be able to construct protein mutants for detailed analysis. EPR was used to control the correct insertion of the cofactors, specifically of the two [Fe2S2] clusters.198... 

Quinoline oxidoreductase Bacterial CC2P2Y2 (MPTpC)Mo(0)(S)bc Unknown 2 Fe2S2, 2 FAD 261... 

Figure 11. Comparison of the EPR powder spectra (20 K) of the two reduced [2Fe2S] clusters FeSI and FeSII of various molybdenum hydroxylases of the xanthine oxidase (XO) family showing a pronounced variation of EPR parameters of the centers. The principal g-tensor components of both clusters are indicated. The horizontal arrows mark appearance of dipolar interaction between the clusters. The dashed rectangle covers the field range of sizeable contributions from paramagnetic Mo(V) species. Qor quinoline oxidoreductase Qox qui-naldine oxidase lor isoquinoline oxidoreductase Mop aldehyde oxidoreductase.

Schach S, B Tshisuaka, S Fetzner, F Lingens F (1995) Quinoline 2-oxidoreductase and 2-oxo-l,2-dihydro-quinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. EurJ Biochem 232 536-544. 

These oxidoreductases are widely used for the introduction of the oxygen atom from HjO into heteroarenes, especially azaarenes including pyridine, quinoline, pyrimidine, and purine, and they generally contain molybdenum. 

The enzymes from Comamonas testosteroni for hydroxylation of quinoline to quinol-2-one (quinoline 2-oxidoreductase) and the dioxygenase responsible for the introduction of oxygen into the benzenoid ring (2-oxo-l,2-dihydroquinoline 5,6-dioxygenase) have been described (Schach et al. 1995). 

The degradation of isoquinoline by Alcaligenes faecalis strain Pa and Pseudomonas diminuta strain 7 (Roger et al. 1990, 1995) is mediated by an oxidoreductase that produces 1,2-dihydroiso-quinoline-l-one, followed by ring fission with the production of o-phthalate and oxidation to 3,4-dihydroxybenzoate (Figure 3.38). The oxidoreductase is purified and like most typical aza-rene oxidoreductases contains, per mole, 0.85 g atoms of Mo, 3.9 g atoms of Fe, and acid-labile S (Lehmann et al. 1994). 

De Beyer A, E Lingens (1993) Microbial metabolism of quinoline and related compounds XVI. Quinaldine oxidoreductase from Arthrobacter spec. Rii 61a a molybdenum-containing enzyme catalysing the hydroxylation at C-4 of the heterocycle. Biol Chem Eloppe-Seyler 374 101-120. 

C. tetosteroni 63 [320,349] Susanne Fetzner Quinoline 2-oxidoreductase (360 kDa) Nitrogen removal (hydroxycoumarin pathway). Reactivity demonstrated with heterocyclic-N... 

Blase, M. Bruntner, C. Tshisuaka, B., et al., Cloning, Expression, and Sequence Analysis of the Three Genes Encoding Quinoline 2-Oxidoreductase, a Molybdenum-Containing Hydroxylase From Pseudomonas Putida 86. J, Biol Chem,. 1996. 271(38) pp. 23068-23079. 

A purine hydroxylase from fungi,639 bacterial quinoline and isoquinoline oxidoreductases,640/641 and a selenium-containing nicotinic acid hydroxylase from Clostridium barberei6i2 are members of the... 

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