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Pterin-oxygen intermediate

In summary, we may add that bacterial utilization of quinoline and its derivatives as a rule depends on the availability of traces of molybdate in the culture medium [363], In contrast, growth of the bacterial strains on the first intermediate of each catabolic pathway, namely, the lH-2-oxo or 1 II-4-oxo derivatives of the quinoline compound was not affected by the availability of molybdate. This observation indicated a possible role of the trace element molybdenum in the initial hydroxylation at C2. In enzymes, Mo occurs as part of the redox-active co-factor, and all the Mo-enzymes involved in N-heteroatomic compound metabolism, contain a pterin Mo co-factor. The catalyzed reaction involves the transfer of an oxygen atom to or from a substrate molecule in a two-electron redox reaction. The oxygen is supplied by the aqueous solvent. Certainly, the Mo-enzymes play an important role in the initial steps of N-containing heterocycles degradation. [Pg.170]


See other pages where Pterin-oxygen intermediate is mentioned: [Pg.318]    [Pg.318]    [Pg.1744]    [Pg.318]    [Pg.262]    [Pg.263]    [Pg.269]    [Pg.286]    [Pg.160]    [Pg.302]    [Pg.710]    [Pg.2258]    [Pg.88]    [Pg.80]    [Pg.632]    [Pg.385]    [Pg.2257]    [Pg.360]    [Pg.169]    [Pg.383]    [Pg.385]    [Pg.332]    [Pg.159]    [Pg.352]   
See also in sourсe #XX -- [ Pg.318 ]




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Oxygenated intermediates

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