JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Weiss, E.
Right arrow Articles by Gaugler, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weiss, E.
Right arrow Articles by Gaugler, R. W.

 Previous Article  |  Next Article 

J Bacteriol. 1968 November; 96(5): 1567-1573
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

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

E. Weiss, E. M. Neptune Jr. and R. W. Gaugler

a Naval Medical Research Institute, Bethesda, Maryland 20014

ABSTRACT

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 {alpha}-ketoglutarate and was reversed by added catalase. Dehydrogenation of {alpha}-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.


FOOTNOTES

1 From the Bureau of Medicine and Surgery, Navy Department, Research Tasks MR005.09.0007 and MF002.03.03-1001.


J Bacteriol. 1968 November; 96(5): 1567-1573
Copyright © 1968 American Society for Microbiology. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1968 by the American Society for Microbiology. All rights reserved.