Arch Microbiology
1991; 155(2):164-9

Molybdenum-dependent degradation of quinoline by Pseudomonas putida Chin IK and other aerobic bacteria

Blaschke M, Kretzer A, Schafer C, Nagel M, Andreesen JR

Institut fur Mikrobiologie der Universitat, Gottingen, Federal Republic of Germany.


Abstract
Eighteen different aerobic bacteria were isolated which utilized quinoline as sole source of carbon, nitrogen, and energy. Attempts were unsuccessful at isolating anaerobic quinoline-degrading bacteria. The optimal concentration of quinoline for growth was in the range of 2.5 to 5 mM. Some organisms excreted 2-hydroxyquinoline as the first intermediate. Hydroxylation of quinoline was catalyzed by a dehydrogenase which was induced in the presence of quinoline or 2-hydroxyquinoline. Quinoline dehydrogenase activity was dependent on the availability of molybdate in the growth medium. Growth on quinoline was inhibited by tungstate, an antagonist of molybdate. Partially purified quinoline dehydrogenase from Pseudomonas putida Chin IK indicated the presence of flavin, iron-sulfur centers, and molybdenum-binding pterin. Mr of quinoline dehydrogenase was about 300 kDa in all isolates investigated.

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