Influence of thiol stress on oxidative phosphorylation and generation of ROS in Streptomyces coelicolor
Hemendra J. Vekaria, Ratna Prabha Chivukula
DOI: 10.4236/jbpc.2010.13020   PDF    HTML     4,577 Downloads   9,553 Views   Citations


Thiols play very important role in the intracellular redox homeostasis. Imbalance in the redox status leads to changes in the intracellular metabolism including respiration. Thiol stress, a reductive type of stress can also cause redox imbalance. When Gram-positive bacterium Strep- tomyces coelicolor was exposed to thiol stress, catalaseA was induced. Induction of catalaseA is the consequence of elevation of ROS (reactive oxygen species). The two major sources of reactive oxygen species are Fenton reaction and slippage of electrons from electron transport chain during respiration. Hence, the effect of thiol stress was checked on the rate of oxidative phosphorylation in S. coelicolor. We found correlation in the increase of oxidative phosphorylation rate and the generation of ROS, subsequently leading to induction of catalase. It was observed that thiol stress does not affect the functionality of the individual complexes of the ETC, but still there was an increase in the overall respiration, which may lead to generation of more ROS leading to induction of catalase.

Share and Cite:

Vekaria, H. and Chivukula, R. (2010) Influence of thiol stress on oxidative phosphorylation and generation of ROS in Streptomyces coelicolor. Journal of Biophysical Chemistry, 1, 172-176. doi: 10.4236/jbpc.2010.13020.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] Van der Beek, E.G. and Stouthamer, A.H. (1973) Oxidative phosphorylation in intact bacteria. Archives of Microbiology, 89, 327-339.
[2] Niebisch, A. and Bott, M. (2003) Purification of a cytochrome bc-aa3 supercomplex with quinol oxidase activity from Corynebacterium glutamicum. Identification of a fourth subunity of cytochrome aa3 oxidase and mutational analysis of diheme cytochrome c1. Journal of Biological Chemistry, 278, 4339-4346.
[3] Schafer, G. and Penefsky, H.S. (2008) Bioenergetics: energy conservation and conversion: Introduction. Results and Problems in Cell Differentiation, 45, IV-VIII.
[4] Kroger, A., Biel, S., Simon, J., Gross, R., Unden, G. and Lancaster, C.R. (2002) Fumarate respiration of Wolinella succinogenes: Enzymology, energetics and coupling mechanism. Biochimica et Biophysica Acta, 1553, 23-38.
[5] Nishimura, T., Vertes, A.A., Shinoda, Y., Inui, M. and Yukawa, H. (2007) Anaerobic growth of Corynebacterium glutamicum using nitrate as a terminal electron acceptor. Applied Microbiology and Biotechnology, 75, 889-897.
[6] Harold, F.M. (1972) Conservation and transformation of energy by bacterial membranes. Bacteriological Reviews, 36, 172-230.
[7] Harold, F.M. (1972) Ion transport and electrogenesis in bacteria. Biochemical Journal, 127, 49-50.
[8] Seaver, L.C. and Imlay, J.A. (2001) Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. Journal of Bacteriology, 183, 7173-7181.
[9] Gonzalez-Flecha, B. and Boveris, A. (1995) Mitochondrial sites of hydrogen peroxide production in reperfused rat kidney cortex. Biochimica et Biophysica Acta, 1243, 361-366.
[10] Gonzalez-Flecha, B. and Demple, B. (1995) Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. Journal of Biological Chemistry, 270, 13681-13687.
[11] Messner, K.R. and Imlay, J.A. (1999) The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. Journal of Biological Chemistry, 274, 10119-10128.
[12] Salunkhe, P., Topfer, T., Buer, J. and Tummler, B. (2005) Genome-wide transcriptional profiling of the steady-state response of Pseudomonas aeruginosa to hydrogen peroxide. Journal of Bacteriology, 187, 2565-2572.
[13] Netto, L.E. and Stadtman, E.R. (1996) The iron-catalyzed oxidation of dithiothreitol is a biphasic process: hydrogen peroxide is involved in the initiation of a free radical chain of reactions. Archives of Biochemistry and Biophysics, 333, 233-242.
[14] Vekaria, H., Sadagopan, K., Adamec, J., Jarori, G.K. and Prabha, C.R. (2007) Thiol stress induces catalaseA in Streptomyces coelicolor. In: Méndez-Vilas, A., Ed., Communicating Current Research and Educational Topics and Trends in Applied Microbiology, Formatex, 246- 254.
[15] Held, K.D. and Biaglow, J.E. (1994) Mechanisms for the oxygen radical-mediated toxicity of various thiol-containing compounds in cultured mammalian cells. Radiation Research, 139, 15-23.
[16] Melvin, R. G. and Ballard, J.W. (2006) Intraspecific variation in survival and mitochondrial oxidative phosphorylation in wild-caught Drosophila simulans. Aging Cell, 5, 225-233.
[17] Stonesifer, J. and Baltz, R.H. (1985) Mutagenic DNA repair in Streptomyces. The Proceedings of the National Academy of Sciences Online (US), 82, 1180-1183.
[18] Aebi, H. (1984) Catalase in vitro. Methods in Enzymology, 105, 121-126.
[19] Cathcart, R., Schwiers, E. and Ames, B.N. (1983) Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Analytical Biochemistry, 134, 111-116.
[20] Richardson, D.J. (2000) Bacterial respiration: A flexible process for a changing environment. Microbiology, 146, 551-571.
[21] Cox, J.S., Shamu, C.E. and Walter, P. (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell, 73, 1197-1206.
[22] Kohno, K., Normington, K., Sambrook, J., Gething, M.J. and Mori, K. (1993) The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Molecular Cell Biology, 13, 877-890.
[23] Huang, L.E., Zhang, H., Bae, S.W. and Liu, A.Y. (1994) Thiol reducing reagents inhibit the heat shock response. Involvement of a redox mechanism in the heat shock signal transduction pathway. Journal of Biological Chemistry, 269, 30718-30725.
[24] Starkebaum, G. and Harlan, J.M. (1986) Endothelial cell injury due to copper-catalyzed hydrogen peroxide generation from homocysteine. Journal of Clinical Investigation, 77, 1370-1376.
[25] Stamler, J.S., Osborne, J.A., Jaraki, O., Rabbani, L.E., Mullins, M., Singel, D. and Loscalzo, J. (1993) Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen. Journal of Clinical Investigation, 91, 308-318.
[26] Loscalzo, J. (1996) The oxidant stress of hyperhomocyst(e) inemia. Journal of Clinical Investigation, 98, 5-7.
[27] Berglin, E. H., Edlund, M.B., Nyberg, G.K. and Carlsson, J. (1982) Potentiation by L-cysteine of the bactericidal effect of hydrogen peroxide in Escherichia coli. Journal of Bacteriology, 152, 81-88.
[28] Park, S. and Imlay, J.A. (2003) High levels of intracellular cysteine promote oxidative DNA damage by driving the fenton reaction. Journal of Bacteriology, 185, 1942- 1950.
[29] Woodmansee, A.N. and Imlay, J.A. (2002) Reduced flavins promote oxidative DNA damage in non-respiring Escherichia coli by delivering electrons to intracellular free iron. Journal of Biological Chemistry, 277, 34055- 34066.
[30] Kachur, A.V., Held, K.D., Koch, C.J. and Biaglow, J.E. (1997) Mechanism of production of hydroxyl radicals in the copper-catalyzed oxidation of dithiothreitol. Radiation Research, 147, 409-415.

Copyright © 2023 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.