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Chapter 5 - Tricarboxylic acid (TCA) cycle, electron transport and oxidative phosphorylation

Published online by Cambridge University Press:  04 May 2019

Byung Hong Kim
Korea Institute of Science and Technology, Seoul
Geoffrey Michael Gadd
University of Dundee
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Publisher: Cambridge University Press
Print publication year: 2019

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Primary Sources

Austin, C. M., Wang, G. & Maier., R. J. (2015). Aconitase functions as a pleiotropic posttranscriptional regulator in Helicobacter pylori. Journal of Bacteriology 197, 30763086.
Bott, M. (2007). Offering surprises: TCA cycle regulation in Corynebacterium glutamicum. Trends in Microbiology 15, 417425.
Hu, Y. & Holden, J. F. (2006). Citric acid cycle in the hyperthermophilic archaeon Pyrobaculum islandicum grown autotrophically, heterotrophically, and mixotrophically with acetate. Journal of Bacteriology 188, 43504355.
Meyer, F. M., Gerwig, J., Hammer, E., Herzberg, C., Commichau, F. M., Völker, U. & Stülke, J. (2011). Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon. Metabolic Engineering 13, 1827.
Pechter, K. B., Meyer, F. M., Serio, A. W., Stülke, J. & Sonenshein, A. L. (2013). Two roles for aconitase in the regulation of tricarboxylic acid branch gene expression in Bacillus subtilis. Journal of Bacteriology 195, 15251537.
van der Rest, M. E., Frank, C. & Molenaar, D. (2000). Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli. Journal of Bacteriology 182, 68926899.
Zhang, S. & Bryant, D. A. (2011). The tricarboxylic acid cycle in cyanobacteria. Science 334, 15511553.

Secondary Sources

Alber, B. E., Spanheimer, R., Ebenau-Jehle, C. & Fuchs, G. (2006). Study of an alternate glyoxylate cycle for acetate assimilation by Rhodobacter sphaeroides. Molecular Microbiology 61, 297309.
Borjian, F., Han, J., Hou, J., Xiang, H., Zarzycki, J. & Berg, I. A. (2017). Malate synthase and β-methylmalyl coenzyme A lyase reactions in the methylaspartate cycle in Haloarcula hispanica. Journal of Bacteriology 199(4).
El-Mansi, M., Cozzone, A. J., Shiloach, J. & Eikmanns, B. J. (2006). Control of carbon flux through enzymes of central and intermediary metabolism during growth of Escherichia coli on acetate. Current Opinion in Microbiology 9, 173179.
Ensign, S. A. (2006). Revisiting the glyoxylate cycle: alternate pathways for microbial acetate assimilation. Molecular Microbiology 61, 274276.
Erb, T. J., Brecht, V., Fuchs, G., Müller, M. & Alber, B. E. (2009). Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase. Proceedings of the National Academy of Sciences of the USA 106, 88718876.
Khomyakova, M., Bükmez, Ö., Thomas, L. K., Erb, T. J. & Berg, I. A. (2011). A methylaspartate cycle in haloarchaea. Science 331, 334337
Leroy, B., De Meur, Q., Moulin, C., Wegria, G. & Wattiez, R. (2015). New insight into the photoheterotrophic growth of the isocitrate lyase-lacking purple bacterium Rhodospirillum rubrum on acetate. Microbiology 161, 10611072.
Sauer, U. & Eikmanns, B. J. (2005). The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria. FEMS Microbiology Reviews 29, 765794.
Brutinel, E. D. & Gralnick, J. A. (2012). Anomalies of the anaerobic tricarboxylic acid cycle in Shewanella oneidensis revealed by Tn-seq. Molecular Microbiology 86, 273283.
Juhnke, H. D., Hiltscher, H., Nasiri, H. R., Schwalbe, H. & Lancaster, C. R. D. (2009). Production, characterization and determination of the real catalytic properties of the putative ‘succinate dehydrogenase’ from Wolinella succinogenes. Molecular Microbiology 71, 10881101.
Miura, A., Kameya, M., Arai, H., Ishii, M. & Igarashi, Y. (2008). A soluble NADH-dependent fumarate reductase in the reductive tricarboxylic acid cycle of Hydrogenobacter thermophilus TK-6. Journal of Bacteriology 190, 71707177.
Amend, J. P. & Shock, E. L. (2001). Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria. FEMS Microbiology Reviews 25, 175243.
Schoepp-Cothenet, B., van Lis, R., Atteia, A., Baymann, F., Capowiez, L., Ducluzeau, A.-L., Duval, S., ten Brink, F., Russell, M. J. & Nitschke, W. (2013). On the universal core of bioenergetics. Biochimica et Biophysica Acta 1827, 7993.
von Stockar, U., Maskow, T., Liu, J., Marison, I. W. & Patino, R. (2006). Thermodynamics of microbial growth and metabolism: an analysis of the current situation. Journal of Biotechnology 121, 517533.
Au, K. M., Barabote, R. D., Hu, K. Y. & Saier, M. H. J. (2006). Evolutionary appearance of H+-translocating pyrophosphatases. Microbiology 152, 12431247.
Capaldi, R. & Aggeler, R. (2002). Mechanism of the F1Fo-type ATP synthase, a biological rotary motor. Trends in Biochemical Sciences 27, 154160.
Ferguson, S. A., Keis, S. & Cook, G. M. (2006). Biochemical and molecular characterization of a Na+-translocating F1Fo-ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum. Journal of Bacteriology 188, 50455054.
Hicks, D. B., Liu, J., Fujisawa, M. & Krulwich, T. A. (2010). F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations. Biochimica et Biophysica Acta 1797, 13621377.
Junge, W. & Nelson, N. (2015). ATP synthase. Annual Review of Biochemistry 84, 631657.
Lapierre, P., Shial, R. & Gogarten, J. P. (2006). Distribution of F- and A/V-type ATPases in Thermus scotoductus and other closely related species. Systematic and Applied Microbiology 29, 1523.
Mulkidjanian, A. Y., Makarova, K. S., Galperin, M. Y. & Koonin, E. V. (2007). Inventing the dynamo machine: the evolution of the F-type and V-type ATPases. Nature Reviews Microbiology 5, 892899.
Schlegel, K., Leone, V., Faraldo-Gómez, J. D. & Müller, V. (2012). Promiscuous archaeal ATP synthase concurrently coupled to Na+ and H+ translocation. Proceedings of the National Academy of Sciences of the USA 109, 947952.
Baker-Austin, C. & Dopson, M. (2007). Life in acid: pH homeostasis in acidophiles. Trends in Microbiology 15, 165171.
Cotter, P. D. & Hill, C. (2003). Surviving the acid test: responses of Gram-positive bacteria to low pH. Microbiology and Molecular Biology Reviews 67, 429453.
Hunte, C., Screpanti, E., Venturi, M., Rimon, A., Padan, E. & Michel, H. (2005). Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. Nature 435, 11971202.
Kanjee, U. & Houry, W. A. (2013). Mechanisms of acid resistance in Escherichia coli. Annual Review of Microbiology 67, 6581.
Krulwich, T. A., Sachs, G. & Padan, E. (2011). Molecular aspects of bacterial pH sensing and homeostasis. Nature Reviews Microbiology 9, 330343.
Lund, P., Tramonti, A. & De Biase, D. (2014). Coping with low pH: molecular strategies in neutralophilic bacteria. FEMS Microbiology Reviews 38, 10911125.
Quinn, M. J., Resch, C. T., Sun, J., Lind, E. J., Dibrov, P. & Häse, C. C. (2012). NhaP1 is a K+(Na+)/H+ antiporter required for growth and internal pH homeostasis of Vibrio cholerae at low extracellular pH. Microbiology 158, 10941105.
Rhee, J. E., Jeong, H. G., Lee, J. H. & Choi, S. H. (2006). AphB influences acid tolerance of Vibrio vulnificus by activating expression of the positive regulator CadC. Journal of Bacteriology 188, 64906497.
Antonyuk, S. V., Han, C., Eady, R. R. & Hasnain, S. S. (2013). Structures of protein–protein complexes involved in electron transfer. Nature 496, 123126.
Arai, H., Kawakami, T., Osamura, T., Hirai, T., Sakai, Y. & Ishii, M. (2014). Enzymatic characterization and in vivo function of five terminal oxidases in Pseudomonas aeruginosa. Journal of Bacteriology 19, 42064215.
Elling, F. J., Becker, K. W., Könneke, M., Schröder, J. M., Kellermann, M. Y., Thomm, M. & Hinrichs, K.-U. (2016). Respiratory quinones in archaea: phylogenetic distribution and application as biomarkers in the marine environment. Environmental Microbiology 18, 692707.
Fadeeva, M. S., Nunez, C., Bertsova, Y. V., Espin, G. & Bogachev, A. V. (2008). Catalytic properties of Na+-translocating NADH:quinone oxidoreductases from Vibrio harveyi, Klebsiella pneumoniae, and Azotobacter vinelandii. FEMS Microbiology Letters 279, 116123.
Lunak, Z. R. & Noel, K. D. (2015). A quinol oxidase, encoded by cyoABCD, is utilized to adapt to lower O2 concentrations in Rhizobium etli CFN42. Microbiology 161, 203212.
Magalon, A., Arias-Cartin, R. & Walburger, A. (2012). Supramolecular organization in prokaryotic respiratory systems. Advances in Microbial Physiology 61, 217266.
Marreiros, B. C., Sena, F. V., Sousa, F. M., Batista, A. P. & Pereira, M. M. (2016). Type II NADH:quinone oxidoreductase family: phylogenetic distribution, structural diversity and evolutionary divergences. Environmental Microbiology 18, 46974709.
Richardson, D. J. (2000). Bacterial respiration: a flexible process for a changing environment. Microbiology 146, 551571.
Richhardt, J., Luchterhand, B., Bringer, S., Büchs, J. & Bott, M. (2013). Evidence for a key role of cytochrome bo3 oxidase in respiratory energy metabolism of Gluconobacter oxydans. Journal of Bacteriology 195, 42104220.
Simon, J. G., van Spanning, R. J. M. & Richardson, D. J. (2008). The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems. Biochimica et Biophysica Acta 1777, 14801490.
Steuber, J., Vohl, G. Casutt, M. S., Vorburger, T., Diederichs, K. & Fritz, G. (2014). Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase. Nature 516, 6267.
Biegel, E. & Müller, V. (2010). Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase. Proceedings of the National Academy of Sciences of the USA 107, 1813818142.
Buckel, W. & Thauer, R. K. (2013). Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation. Biochimica et Biophysica Acta 1827, 94113.
Hedderich, R. (2004). Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. Journal of Bioenergetics and Biomembranes 36: 6575.
Kim, B. H., Lim, S. S., Daud, W. R. W., Gadd, G. M. & Chang, I. S. (2015). The biocathode of microbial electrochemical systems and microbially-influenced corrosion. Bioresource Technology 190, 395401.
Lyell, N. L., Colton, D. M., Bose, J. L., Tumen-Velasquez, M. P., Kimbrough, J. H. & Stabb, E. V. (2013). Cyclic AMP receptor protein regulates pheromone-mediated bioluminescence at multiple levels in Vibrio fischeri ES114. Journal of Bacteriology 195, 50515063.

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