Influence of Gas Environment on Catabolic Activities and on Reoxidation of Reduced Nicotinamide Adenine Dinucleotide Phosphate in Chlamydia1

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We investigated the effect of the gas environment on the enzymatic reactions of intact isolated cells of the agents of trachoma and of meningopneumonitis of the host-dependent genus Chlamydia. In comparison with the reactions taking place in a gas phase of air, O2 depressed CO2 production from pyruvate and glutamate by trachoma and from glutamate by meningopneumonitis. O2 enhanced the degradation of pyruvate by meningopneumonitis, but this effect was due to increased H2O2, and was reversed by added catalase. Both dehydrogenation of α-ketoglutarate and was reversed by added catalase. Dehydrogenation of α-ketoglutarate by both agents and production of CO2 from C1 of glucose-6-phosphate were stimulated by O2 and depressed in N2. The latter activity was stimulated in air, O2, and N2 by nicotinamide adenine dinucleotide phosphate (NADP) in relation to the amount added, and also in air or O2, but not in N2, by moderate amounts of NADP and an excess of oxidized glutathione with concomitant formation of H2O2. A small but significant amount of O2 was consumed during the course of these reactions. It is suggested that glutathione reductase activity can occur only when accompanied by an oxidative reaction, and that this close link between the two reactions represents a mechanism of electron transport which transfers hydrogen to molecular O2.

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