This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lester, R. L. Articles by DeMoss, J. A. Search for Related Content PubMed PubMed Citation Articles by Lester, R. L. Articles by DeMoss, J. A.

 Previous Article  |  Next Article 

J Bacteriol. 1971 March; 105(3): 1006-1014
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Effects of Molybdate and Selenite on Formate and Nitrate Metabolism in Escherichia coli

^a Department of Biology, University of California, La Jolla, California 92037

ABSTRACT

The effects of adding molybdate and selenite to a glucose-minimal salts medium on the formation of enzymes involved in the anaerobic metabolism of formate and nitrate in Escherichia coli have been studied. When cells were grown anaerobically in the presence of nitrate, molybdate stimulated the formation of nitrate reductase and a b-type cytochrome, resulting in cells that had the capacity for active nitrate reduction in the absence of formate dehydrogenase. Under the same conditions, selenite in addition to molybdate was required for forming the enzyme system which permits formate to serve as an effective electron donor for nitrate reduction. When cells were grown anaerobically on a glucose-minimal salts medium without nitrate, active hydrogen production from formate as well as formate dehydrogenase activity depended on the presence of both selenite and molybdate. The effects of these metals on the formation of formate dehydrogenase was blocked by chloramphenicol, suggesting that protein synthesis is required for the increases observed. It is proposed that the same formate dehydrogenase is involved in nitrate reduction, hydrogen production, and in aerobic formate oxidation.

¹ On leave, Department of Biochemistry, University of Kentucky, Lexington, Ky. 40506.

This article has been cited by other articles:

• Magalon, A., Frixon, C., Pommier, J., Giordano, G., Blasco, F. (2002). In Vivo Interactions between Gene Products Involved in the Final Stages of Molybdenum Cofactor Biosynthesis in Escherichia coli. J. Biol. Chem. 277: 48199-48204 [Abstract] [Full Text]  
• Stadtman, T. C. (1974). Selenium Biochemistry: Proteins containing selenium are essential components of certain bacterial and mammalian enzyme systems. Science 183: 915-922 [Abstract]