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 Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wimpenny, J. W. T. Articles by Firth, A. Search for Related Content PubMed PubMed Citation Articles by Wimpenny, J. W. T. Articles by Firth, A.

Levels of Nicotinamide Adenine Dinucleotide and Reduced Nicotinamide Adenine Dinucleotide in Facultative Bacteria and the Effect of Oxygen

Department of Microbiology, University College, Newport Road, Cardiff, Wales

ABSTRACT

Nicotinamide adenine dinucleotide (NAD) and reduced NAD (NADH) levels have been measured in bacterial cultures. The cofactors were assayed by using the very sensitive cycling assay described previously by Cartier. Control experiments showed that the level of total NAD(H) falls during harvesting, and so samples were taken quickly from growing cultures and extracted immediately without separating the cells from the medium. Total NAD(H) ranged from 4.0 to 11.7 µmoles/g of dry cells for three facultative organisms, Klebsiella aerogenes, Escherichia coli, and Staphylococcus albus. NADH was remarkably constant in these bacteria; only one out of ten series of determinations was outside the range 1.4 to 1.9 µmoles/g of dry cells. NAD⁺ showed much greater variation. An anaerobe (Clostridium welchii) had significantly more total NAD(H) whereas an aerobe Pseudomonas aeruginosa had about as much NAD(H) as the facultative organisms. NAD and NADH were measured during growth: once more NADH was much more constant than NAD. During change-over between aerobiosis and anaerobiosis, NADH showed a temporary increase but then returned to a constant level, whereas NAD changed from high aerobically to low anaerobically. These results are discussed in terms of the control mechanisms that may be involved.

This article has been cited by other articles:

• Price-Whelan, A., Dietrich, L. E. P., Newman, D. K. (2007). Pyocyanin Alters Redox Homeostasis and Carbon Flux through Central Metabolic Pathways in Pseudomonas aeruginosa PA14. J. Bacteriol. 189: 6372-6381 [Abstract] [Full Text]  
• Nakamura, S., Oda, M., Kataoka, S., Ueda, S., Uchiyama, S., Yoshida, T., Kobayashi, Y., Ohkubo, T. (2006). Apo- and Holo-structures of 3{alpha}-Hydroxysteroid Dehydrogenase from Pseudomonas sp. B-0831: LOOP-HELIX TRANSITION INDUCED BY COENZYME BINDING. J. Biol. Chem. 281: 31876-31884 [Abstract] [Full Text]  
• Grose, J. H., Joss, L., Velick, S. F., Roth, J. R. (2006). Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress. Proc. Natl. Acad. Sci. USA 103: 7601-7606 [Abstract] [Full Text]  
• Causey, T. B., Shanmugam, K. T., Yomano, L. P., Ingram, L. O. (2004). Engineering Escherichia coli for efficient conversion of glucose to pyruvate. Proc. Natl. Acad. Sci. USA 101: 2235-2240 [Abstract] [Full Text]  
• Neves, A. R., Ventura, R., Mansour, N., Shearman, C., Gasson, M. J., Maycock, C., Ramos, A., Santos, H. (2002). Is the Glycolytic Flux in Lactococcus lactis Primarily Controlled by the Redox Charge? KINETICS OF NAD+ AND NADH POOLS DETERMINED IN VIVO BY 13C NMR. J. Biol. Chem. 277: 28088-28098 [Abstract] [Full Text]  
• Abreu, I. A., Saraiva, L. M., Soares, C. M., Teixeira, M., Cabelli, D. E. (2001). The Mechanism of Superoxide Scavenging by Archaeoglobus fulgidus Neelaredoxin. J. Biol. Chem. 276: 38995-39001 [Abstract] [Full Text]  
• Desvaux, M., Guedon, E., Petitdemange, H. (2001). Carbon Flux Distribution and Kinetics of Cellulose Fermentation in Steady-State Continuous Cultures of Clostridium cellulolyticum on a Chemically Defined Medium. J. Bacteriol. 183: 119-130 [Abstract] [Full Text]  
• Boonstra, B., Rathbone, D. A., French, C. E., Walker, E. H., Bruce, N. C. (2000). Cofactor Regeneration by a Soluble Pyridine Nucleotide Transhydrogenase for Biological Production of Hydromorphone. Appl. Environ. Microbiol. 66: 5161-5166 [Abstract] [Full Text]  
• Guedon, E., Payot, S., Desvaux, M., Petitdemange, H. (1999). Carbon and Electron Flow in Clostridium cellulolyticum Grown in Chemostat Culture on Synthetic Medium. J. Bacteriol. 181: 3262-3269 [Abstract] [Full Text]  
• Steuber, J., Krebs, W., Bott, M., Dimroth, P. (1999). A Membrane-Bound NAD(P)+-Reducing Hydrogenase Provides Reduced Pyridine Nucleotides during Citrate Fermentation by Klebsiella pneumoniae. J. Bacteriol. 181: 241-245 [Abstract] [Full Text]  
• Unkefer, C., Blazer, R., London, R. (1983). In vivo determination of the pyridine nucleotide reduction charge by carbon-13 nuclear magnetic resonance spectroscopy. Science 222: 62-65 [Abstract]