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Chapter 14 : Respiratory Chains

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Abstract:

This chapter briefly reviews some major aspects of the physiology, biochemistry, and molecular genetics of respiratory chains currently under active study and to suggest some neglected areas to which effort could be directed. It reflects the author's biases, but the references lead the diligent reader to a fuller or more balanced treatment of certain issues. Membrane-bound respiratory chains catalyze the transfer of reducing equivalents from a reduced substrate to an oxidant. This transfer is spontaneous and is based on differences in oxidation-reduction potential among the members of the chain. The usage of menaquinone (to the exclusion of ubiquinone), for example, not only in all gram-positive bacteria but also in the majority of archaebacteria suggests that formation of the unique features of bacterial respiratory chains constituted a very early event in the evolutionary development of cellular biochemistry. In terms of total electron flow through the respiratory chain, the two most important dehydrogenases are those responsible for oxidizing succinate and NADH. As work with respiratory chains progresses to studies of the molecular nature of the complex, NADH dehydrogenase, cytochrome , and cytochrome , undoubtedly there will be further structural and functional similarities to well-studied bacteria such as . Indeed, the paths for electron flow through respiratory chains to oxygen have remarkable similarities to those in the .

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14

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Figures

Image of Figure 1
Figure 1

Structures of hemes found in bacterial cytochromes. In heme D, the 8,9 double bond is saturated to create a dihydroporphyrin (chlorin) ring structure. The group at C-2 of heme A is hydroxyethylfarnesyl. Heme ? has been proposed ( ) to have a grouping at C-2 similar to that of heme A but with a methyl rather than a formyl group at C-l.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Image of Figure 2
Figure 2

Gene-enzyme relationships in the biosynthesis of uroporphyrinogen III (UroIII) from glutamate (Glu) in ( ). Protoporphyrin is formed from UroIII by sequential decarboxylation and dehydrogenation reactions, and protoheme is formed from protoporphyrin by incorporation of Fe. Enzyme 1, glutamyl-tRNA synthase; enzyme 2, NAD(P)H:glutamyl-tRNA reductase; enzyme 3, glutamate-1-semialdehyde (GSA) 2,1-aminotransferase; enzyme 4, porphobilinogen (PBG) synthase; enzyme 5, hydroxymethylbilane (HMB) synthase; enzyme 6, UroIII synthase. ALA, 5-aminoIevulinic acid.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Image of Figure 3
Figure 3

Organization of the gene cluster (based on data in reference ). Gene functions are as given in Fig. 2 . P, promoter.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Image of Figure 4
Figure 4

Organization of the and genes in ( ). The gene constitutes a verified monocistronic transcriptional unit ( ), while the and transcripts are inferred from localization of putative promoter sequences. Arrangement of the genes appears to be similar in the thermophilic sp. strain PS3 ( ) and the alkaliphile ( ).

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Image of Figure 5
Figure 5

. Gene-enzyme relationships in the biosynthesis of menaquinone from chorismate in This scheme is in part based on results from but the relationships appear to be identical in both species. menaquinone-specific isochorismate synthase; menaquinone-specific 2-ketoglutarate dehydrogenase; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; o-succinylbenzoic acid synthase; o-succinylbenzoic acid coenzyme A synthetase; l,4-dihydroxy-2-naphthoic acid synthase; polyisoprenyl transferase; SAM, S-adenosylmethionine; TPP, thiamine pyrophosphate anion; CoA-SH, coenzyme A-sulfhydryl; RPP, polyisoprenyl pyrophosphate; and SAH, S-adenosyl-homocysteine. R' and R” in OSB-CoA denote the positional indeterminacy of CoA-SH.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Figure 6

Sequence and transcriptional organization of the gene cluster in ( ). The and gene functions are shown in Fig. 4 and 5 ; open reading frames 1, 5, and 8 have not been identified with specific enzymatic activities. Bold arrows denote experimentally established sites of transcription initiation; light arrows indicate sites inferred from integrational disruption experiments. See text for details.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Image of Figure 7
Figure 7

Metabolic relationship of menaquinone biosynthesis to formation of dihydroxybenzoic acid-based iron-chelating compounds in A similar scheme can be drawn for with replacing For abbreviations, see the legend to Fig. 5 . PABA, -aminobenzoic acid.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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Figure 8

Possible paths for aerobic electron transfer in the bacilli. See the text for discussion.

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14
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References

/content/book/10.1128/9781555818388.chap14
1. Anemüller, S.,, and G. Schâfer. 1989. Cytochrome aa3 from the thermoacidophilic archaebacterium Sulfolobus aeidocaldarius. FEBS Lett. 244:451455.
2. Anraku, Y. 1988. Bacterial electron transfer chains. Annu. Rev. Biochem. 57:101132.
3. Anraku, Y.,, and R. B. Gennis. 1987. The aerobic respiratory chain of Escherichia coli. Trends Biochem. Sci. 12:262266.
4. Anthony, C. (ed.) 1988. Bacterial Energy Transduction. Academic Press, Inc., New York.
5. Arrow, A. S.,, and H. W. Taber. 1986. Streptomycin accumulation by Bacillus subtilis requires both a membrane potential and cytochrome aa3. Antimicrob. Agents Chemother. 29:141146.
6. Bentley, R.,, and R. Meganathan,. 1987. Biosynthesis of the isoprenoid quinones ubiquinone and menaquinone, p. 512520. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 1. American Society for Microbiology, Washington, D.C.
7. Berek, I.,, A. Miczak,, and G. Ivanovics. 1974. Mapping of the delta-aminolevulinic acid dehydrase and porpho-bilinogen deaminase loci in Bacillus subtilis. Mol. Gen. Genet. 132:233239.
8. Berek, I.,, A. Miczak,, I. Kiss,, G. Ivanovics,, and I. Durko. 1975. Genetic and biochemical analysis of hemin dependent mutants of Bacillus subtilis. Acta Microbiol. Acad. Sci. Hung. 22:157167.
9. Bergsma, J.,, M. B. M. van Dongen,, and W. N. Konings. 1982. Purification and characterization of NADH dehydrogenase from Bacillus subtilis. Eur. J. Biochem. 128: 151157.
10. Bergsma, J.,, K. E. Melhuizen,, W. van Oeveren,, and W. N. Konings. 1982. Restoration of NADH oxidation with menaquinones and menaquinone analogues in membrane vesicles from the menaquinone-dencient Bacillus subtilis aroD. Eur. J. Biochem. 125:651657.
11. Bergsma, J.,, R. Strijker,, J. Y. E. Alkema,, H. G. Seljen,, and W. N. Konings. 1981. NADH dehydrogenase and NADH oxidation in membrane vesicles from Bacillus subtilis. Eur. J. Biochem. 120:599606.
12. Bisschop, A.,, and W. N. Konings. 1976. Reconstitution of reduced nicotinamide adenine dinucleotide oxidase activity with menadione in membrane vesicles from the menaquinone-deficient Bacillus subtilis aroD. Relation between electron transfer and active transport. Eur. J. Biochem. 67:357365.
13. Broberg, P. L.,, and L. Smith. 1967. The cytochrome system of Bacillus megaterium KM. The presence and properties of two CO-binding cytochromes. Biochim. Biophys. Acta 131:479489.
14. Castor, L. N.,, and B. Chance. 1959. Photochemical determinations of the oxidases of bacteria. J. Biol. Chem. 234:15871592.
15. Chaix, P.,, and J. F. Petit. 1956. Etude des différents spectres cytochromique de Bacillus subtilis. Biochim. Biophys. Acta 22:6671.
16. Chaix, P.,, and J. F. Petit. 1957. Influence du taux de croissance sur la constitution du spectra hématinique de Bacillus subtilis. Biochim. Biophys. Acta 25:481486.
17. Chepuri, V.,, L. J. Lemieux,, D. C.-T. Au,, and R. B. Gennis. 1990. The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of the cytochrome c oxidases. J. Biol. Chem. 265:1118511192.
18. Collins, M. D.,, and D. Jones. 1981. Distribution of isoprenoid quinone structure types in bacteria and their taxonomie implications. Microbiol. Rev. 45:316354.
19. Collins, M. D.,, and T. A. Langworthy. 1983. Respiratory quinone composition of some acidophilic bacteria. Syst. Appl. Microbiol. 4:295304.
20. Davidson, M. W.,, K. A. Gray,, D. B. Knaff,, and T. A. Krulwich. 1988. Purification and characterization of two soluble cytochromes from the alkalophile Bacillus firmus RAB. Biochim. Biophys. Acta 933:470477.
21. De Vrij, W.,, A. Azzi,, and W. N. Konings. 1983. Structural and functional properties of cytochrome c oxidase iron Bacillus subtilis W23. Eur. J. Biochem. 131:97103.
22. De Vrij, W.,, A. J. M. Driessen,, K. J. Hellingwerf,, and W. N. Konings. 1986. Measurements of the protonmotive force generated by cytochrome c oxidase from Bacillus subtilis in proteoliposomes and membrane vesicles. Eur. J. Biochem. 156:431440.
23. De Vrij, W.,, R. I. R. Heyne,, and W. N. Konings. 1989. Characterization and application of a thermostable primary transport system: cytochrome c oxidase from Bacillus stearothermophilus. Eur. J. Biochem. 178:763770.
24. De Vrij, W.,, and W. N. Konings. 1987. Kinetic characterization of cytochrome c oxidase from Bacillus subtilis. Eur. J. Biochem. 166:581587.
25. De Vrij, W.,, B. Poolman,, W. N. Konings,, and A. Azzi. 1986. Purification, enzymatic properties and reconstitution of cytochrome c oxidase from Bacillus subtilis. Methods Enzymol. 126:159173.
26. De Vrij, W.,, B. van den Burg,, and W. N. Konings. 1987. Spectral and potentiometric analysis of cytochromes from Bacillus subtilis. Eur. J. Biochem. 166:589595.
27. Downey, R. J. 1966. Nitrate reductase and respiratory adaptation in Bacillus stearothermophilus. J. Bacteriol. 91:634641.
28. Driscoll, J. R.,, and H. W. Taber. 1992. Sequence organization and regulation of the Bacillus subtilis menBE operon. J. Bacteriol. 174:50635071.
29. Escamllla, J. E.,, B. Barquera,, R. Ramirez,, A. Garcia-Horsman,, and P. Del Arenal. 1988. Role of menaquinone in inactivation and activation of the Bacillus cereus forespore respiratory system. J. Bacteriol. 170: 59085912.
30. Escamllla, J. E.,, and M. C. Benito. 1984. Respiratory system of vegetative and sporulating Bacillus cereus. J. Bacteriol. 160:473477.
31. Escamllla, J. E.,, R. Ramirez,, P. Del Arenal,, and A. Aranda. 1986. Respiratory systems of the Bacillus cereus mother cell and forespore. J. Bacteriol. 167:544550.
32. Escamllla, J. E.,, R. Ramirez,, I. P. Del Arenal,, G. Zarzoza,, and V. Linares. 1987. Expression of cytochrome oxidases in Bacillus cereus: effects of oxygen tension and carbon source. J. Gen. Microbiol. 133:35493555.
33. Farrand, S. K.,, and H. W. Taber. 1973. Pleiotropic menaquinone-deficient mutant of Bacillus subtilis. J. Bacteriol. 115:10211034.
34. Farrand, S. K.,, and H. W. Taber. 1973. Physiological effects of menaquinone deficiency in Bacillus subtilis. J. Bacteriol. 115:10351044.
35. Farrand, S. K.,, and H. W. Taber. 1974. Changes in menaquinone concentration during growth and early sporulation in Bacillus subtilis. J. Bacteriol. 117:324326.
36. Frade, R.,, and P. Chaix. 1973. Influence du pH sur la synthèse de 1'oxidase (cytochrome a3) chez Bacillus coagulans, microorganisme thermophile, capable d' "adaptation respiratoire." Biochim. Biophys. Acta 325: 424432.
37. Frade, R.,, and P. Chaix. 1976. Etude du mécanisme de l'influence du pH extracellulaire sur la synthèse du complexe oxydasique (cytochromes a + a3) chez Bacillus coagulans: relation avec "l'effet glucose" et rôle de la coproporphyrine III excrétée. Biochim. Biophys. Acta 423:573585.
38. Freese, E. B. 1973. Unusual membranous structures in cytochrome a-deficient mutants of Bacillus subtilis. J. Gen. Microbiol. 75:187190.
39. Friden, H.,, and L. Hederstedt. 1990. Role of His residues in Bacillus subtilis cytochrome b-558 for haem binding and assembly of succinate:quinone oxidore-ductase (complex II). Mol. Microbiol. 4:10451056.
40. Garcia-Horsman, J. A.,, B. Barquera,, and J. E. Escamllla. 1991. Two different aa3-type cytochromes can be purified from the bacterium Bacillus cereus. Eur. J. Biochem. 199:761768.
41. Garcia-Horsman, J. A.,, B. Barquera,, D. Gonzalez-Halphen,, and J. E. Escamllla. 1991. Purification and characterization of two-subunit cytochrome aa3 from Bacillus cereus. Mol. Microbiol. 5:197205.
42. Gennis, R. B. 1991. Some recent advances relating to prokaryotic cytochrome c reductases and cytochrome c oxidases. Biochim. Biophys. Acta 1058:2124.
43. Goodman, S. R.,, B. L. Marrs,, R. J. Narconis,, and R. E. Olson. 1976. Isolation and description of a menaquinone mutant from Bacillus licheniformis. J. Bacteriol. 125:282289.
44. Guffanti, A. A.,, and T. A. Krulwich. 1992. A model for a non-chemiosmotic mode of energization of oxidative phosphorylation by alkaliphilic Bacillus firmus OF4. Personal communication.
45. Haddock, B. A.,, and W. A. Hamilton (ed.). 1977. Microbial Energetics. Society for General Microbiology Symposium, vol. 27. Cambridge University Press, Cambridge.
46. Haltia, T.,, M. Finel,, N. Harms,, T. Nakari,, M. Raitlo,, M. Wikstrom,, and M. Saraste. 1989. Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase. EMBO J. 8:35713579.
47. Hansson, M.,, L. Rutberg,, I. Schroder,, and L. Hederstedt. 1991. The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III. J. Bacteriol. 173:25902599.
48. Hederstedt, L. 1986. Molecular properties, genetics and biosynthesis of Bacillus subtilis succinate dehydrogenase complex. Methods Enzymol. 126:399414.
49. Hicks, D. B.,, R. J. Plass,, and P. G. Quirk. 1991. Evidence for multiple terminal oxidases, including cytochrome d, in facultatively alkaliphilic Bacillus firmus OF4.7. Bacteriol. 173:50105016.
50. Hill, K. F.,, J. P. Mueller,, and H. W. Taber. 1990. The Bacillus subtilis menCD promoter is responsive to extracellular pH. Arch. Microbiol. 153:355359.
51. Hogarth, C.,, J. J. Wilkinson,, and D. J. Ellar. 1977. Cyanide resistant electron transport in sporulating Bacillus megaterium KM. Biochim. Biophys. Acta 461:109123.
52. Ishizuka, M.,, K. Machlda,, S. Shimada,, A. Magi,, T. Tsuchiya,, T. Ohmorl,, Y. Suoma,, M. Gonda,, and N. Sone. 1990. Nucleotide sequence of the genes coding for four subunits of cytochrome c oxidase from the thermophilic bacterium PS3. J. Biochem. 108:866873.
53. Ivey, D. M.,, D. B. Hicks,, A. A. Guffantl,, G. Sobel,, and T. A. Krulwich. 1990. The problem of the electrochemical proton potential in alkaliphilic bacteria. Mosbach Colloq. 41:105113.
54. James, W. S.,, F. Gibson,, P. Taronl,, and R. K. Poole. 1989. The cytochrome oxidases of Bacillus subtilis: mapping of a gene affecting cytochrome aa3 and its replacement by cytochrome o in a mutant strain. FEMS Microbiol. Lett. 58:277282.
55. Jones, C. W., 1977. Aerobic respiratory systems in bacteria, p. 2359. In B. A. Haddock, and W. A. Hamilton (ed.), Microbiol Energetics. Society for General Microbiology Symposium, vol. 27. Cambridge University Press, Cambridge.
56. Jones, C. W., 1987. Membrane-associated energy conservation in bacteria: a general introduction, p. 182. In C. Anthony (d.), Bacterial Energy Transduction. Academic Press, Inc., New York.
57. Kaiser, A.,, and E. Leistner. 1990. Role of the entC gene in enterobactin and menaquinone biosynthesis in Escherichia coli. Arch. Biochem. Biophys. 276:331335.
58. Keilin, D. 1925. On cytochrome, a respiratory pigment, common to animals, yeast, and higher plants. Proc. R. Soc.Ser. 5 98:312339.
59. Keilin, D. 1929. Cytochrome and respiratory enzymes. Proc. R. Soc. Ser. B. 104:206252.
60.Keilin, D. 1966. The History of Cell Respiration and Cytochrome. Cambridge University Press, Cambridge.
61. Kell, D. B., 1987. Protonmotive energy-transducing systems: some physical principles and experimental approaches, p. 429490. In C. Anthony (ed.), Bacterial Energy Transduction. Academic Press, Inc., New York.
62. Ketchum, P. A.,, G. Denaniaz,, J. LeGall,, and W. J. Payne. 1991. Menaquinol-nitrate oxidoreductase of Bacillus halodenitrificans. J. Bacteriol. 173:24982505.
63. Kltada, M.,, and T. A. Krulwich. 1984. Purification and characterization of the cytochrome oxidase from alkaliphilic Bacillus firmus RAB. J. Bacteriol. 158:963966.
64. Krulwich, T. A. (ed.). 1990. The Bacteria, vol. XII. Bacterial Energetics. Academic Press, Inc., New York.
65. Krulwich, T. A.,, and A. A. Guffantl. 1989. Alkalophilic bacteria. Annu. Rev. Microbiol. 43:435463.
66. Krulwich, T. A.,, and A. A. Guffantl. 1989. The Na+ cycle of extreme alkalophiles: a secondary Na+/H+ antiporter and Na+/solute symporters. J. Bioenerg. Bio-membr. 21:663677.
67. Krulwich, T. A.,, D. B. Hicks,, D. Seto-Young,, and A. A. Guffantl. 1988. The bioenergetics of alkalophilic bacilli. Crit. Rev. Microbiol. 16:1536.
68. Lauraeus, M.,, T. Haltia,, M. Saraste,, and M. Wikstrom. 1991. Bacillus subtilis expresses two kinds of haem A-containing terminal oxidases. Eur. J. Biochem. 197: 699705.
69. Lemma, E.,, C. Hagerhall,, V. Gelsler,, U. Brandt,, G. von Jagow,, and A. Kröger. 1991. Reactivity of the Bacillus subtilis succinate dehydrogenase complex with quinones. Biochim. Biophys. Acta 1059:281285.
70. Lin, E. C. C.,, and D. R. Kuritzkas,. 1987. Pathways for anaerobic electron transport, p. 201221. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 1. American Society for Microbiology, Washington, D.C.
70a. Lübben, M.,, B. Kolmerer,, and M. Saraste. 1992. An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes. EMBO J. 11:805812.
71. Ludwig, B. 1987. Cytochrome c oxidase in prokaryotes. FEMS Microbiol. Rev. 46:4156.
72. Maloney, P.,C. 1987. Coupling to an energized membrane: role of ion-motive gradients in the transduction of metabolic energy, p. 222243. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 1. American Society for Microbiology, Washington, D.C.
73. Mather, M. W.,, P. Springer,, and J. A. Fee. 1991. Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence and analysis of the deduced primary structure of subunit He of cytochrome caa3. J. Biol. Chem. 266:50255035.
74. McEnroe, A. S.,, and H. W. Taber. 1984. Correlation between cytochrome aa3 concentrations and streptomycin accumulation in Bacillus subtilis. Antimicrob. Agents Chemother. 26:507512.
75. Meganathan, R.,, R. Bentley,, and H. Taber. 1981. Identification of Bacillus subtilis men mutants which lack o-succinylbenzoyl-coenzyme A synthetase and dihydroxynaphthoate synthase. J. Bacteriol. 145:328332.
75a. Meganathan, R.,, and M. Hudspeth. Personal communication.
76. Micznk, A.,, I. Berek,, and G. Ivànovics. 1976. Mapping the uroporphyrinogen decarboxylase, coproporphyrinogen oxidase and ferrochetalase loci in Bacillus subtilis. Mol. Gen. Genet. 146:8587.
77. Miczák, A.,, B. Prágai,, and I. Berek. 1979. Mapping the uroporphyrinogen III cosynthase locus in Bacillus subtilis. Mol. Gen. Genet. 174:293295.
78. Mild, K.,, and K. Okunukl. 1969. Cytochromes of Bacillus subtilis. Purification and spectral properties of cytochromes c-550 and c-554. J. Biochem. 66:831854.
79. Miller, P.,, J. Mueller,, K. H1U,, and H. Taber. 1988. Transcriptional regulation of a promoter in the men gene cluster of Bacillus subtilis. J. Bacteriol. 170:27422748.
80. Miller, P.,, A. Rablnowltz,, and H. Taber. 1988. Molecular cloning and preliminary genetic analysis of the men gene cluster of Bacillus subtilis. J. Bacteriol. 170:27352741.
81. Mueller, J. P.,, and H. W. Taber,. 1988. Genetic regulation of cytochrome aa3 in Bacillus subtilis, p. 9195. In A. T. Ganesan, and J. A. Hoch (ed.), Genetics and Biotechnology of Bacilli, vol. 2. Academic Press, Inc., New York.
82. Mueller, J. P.,, and H. W. Taber. 1989. Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis. J. Bacteriol. 171:49674978.
83. Mueller, J. P.,, and H. W. Taber. 1989. Structure and expression of the cytochrome aa3 controlling gene ctaA of Bacillus subtilis. J. Bacteriol. 171:49794986.
84. Neidhardt, F. C.,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.). 1987. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. American Society for Microbiology, Washington, D.C.
85. Nicholls, P.,, and N. Sone. 1984. Kinetics of cytochrome c and TMPD oxidation by cytochrome c oxidase from the thermophilic bacterium PS3. Biochim. Biophys. Acta 767:240247.
86. O'Neill, G. P.,, M.-W. Chen,, and D. Soil. 1989. Delta-aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiol. Lett. 60:255260.
87. Petricek, M.,, L. Rutberg,, I. Schroder,, and L. Heder-stedt. 1990. Cloning and characterization of the hemA region of the Bacillus subtilis chromosome. J. Bacteriol. 172:22502258.
88. Plggot, P. J., 1989. Revised genetic map of Bacillus subtilis 168, p. 141. In I. Smith,, R. A. Slepecky,, and P. Setlow (ed.), Regulation of Procaryotic Development. American Society for Microbiology, Washington, D.C.
89. Poole, R. K. 1981. Ligand-binding cytochromes a3, c and o in membranes from the thermophilic bacterium PS3. FEBS Lett. 133:255259.
90. Poole, R. K. 1983. Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins. Biochim. Biophys. Acta 726:205243.
91. Poole, R. K., 1988. Bacterial cytochrome oxidase, p. 231291. In C. Anthony (ed.), Bacterial Energy Transduction. Academic Press, Inc., New York.
92. Poole, R. K.,, and W. J. Ingledew,. 1987. Pathways of electrons to oxygen, p. 170200. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 1. American Society for Microbiology, Washington, D.C.
93. Puustinen, A.,, M. Finel,, T. Haltla,, R. P. Gennis,, and M. Wikström. 1991. Properties of the two terminal oxidases of Escherichia coli. Biochemistry 30:39363942.
94. Puustinen, A.,, and M. Wikström. 1991. The heme groups of cytochrome o from Escherichia coli. Proc. Natl. Acad. Set. USA 88:61226126.
94a. Qin, X.,, and H. Taber. Unpublished data.
95. Quirk, P. G.,, A. A. Guffanti,, and T. A. Krulwlch. 1992. Cloning and characterization of genes encoding the caa3-type terminal oxidase from alkaliphilic Bacillus firmus OF4. Abstr. Annu. Meet. Biophys. Soc., p. A285.
96. Quirk, P. G.,, A. A. Guffanti,, R. J. Plass,, S. Clejan,, and T. A. Krulwlch. 1991. Protonophore-resistance and cytochrome expression in mutant strains of the facultative alkaliphile Bacillus firmus OF4. Biochim. Biophys. Acta 1058:131140.
97. Qureshi, M. H.,, I. Yomoto,, T. Fujiwara,, Y. Fukumori,, and T. Yamana. 1990. A novel aco-type cytochrome-c oxidase from a facultative alkalophilic Bacillus: purification, and some molecular and enzymatic features. J. Biochem. 107:480485.
98. Raitio, M.,, J. M. Pispa,, T. Metso,, and M. Saraste. 1990. Are there isoenzymes of cytochrome c oxidase in Paracococcus denitrificans? FEBS Lett. 261:431435.
98a. Rowland, B. Unpublished data.
98b. Rowland, B., et al. Unpublished data.
99. Santana, M.,, F. Kunst,, M. F. Hullo,, G. Rapoport,, A. Danchin,, and P. Glaser. 1992. Molecular cloning, sequencing and physiological characterization of the qox operon from Bacillus subtilis, encoding the aa3-600 quinol oxidase. J. Biol. Chem. 267:1022510231.
100. Saraste, M. 1990. Structural features of cytochrome oxidase. Q. Rev. Biophys. 23:331366.
101. Saraste, M.,, L. Holm,, L. Lemieux,, M. Lubben,, and J. van der Oost. 1991. The happy family of cytochrome oxidases. Biochem. Soc. Trans. 19:608612.
102. Saraste, M.,, T. Metso,, T. Nakari,, T. Jalli,, M. Lauraeus,, and J. van der Oost. 1991. The Bacillus subtilis cytochrome c oxidase. Variations on a conserved theme. Eur. J. Biochem. 195:517525.
103. Saraste, M.,, M. Raitio,, T. Jalli,, V. Chepuri,, L. Lemieux,, and R. B. Gennis. 1988. Cytochrome o from Escherichia coli is structurally related to cytochrome aa3. Ann. N.Y. Acad. Sci. 550:314324.
104. Schroder, I.,, L. Hederstedt,, C. G. Kannangara,, and S. P. Gough. 1992. Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product. Biochem. J. 281:843850.
105. Shapleigh, J. P.,, and R. B. Gennis. 1992. Cloning, sequencing and deletion from the chromosome of the gene encoding subunit I of the aa3-type cytochrome c oxidase of Rhodobacter sphaeroides. Mol. Microbiol. 6:635642.
106. Sharma, V.,, K. Suvarna,, R. Meganathan,, and M. E. S. Hudspeth. 1992. Menaquinone (vitamin K2) biosynthesis: nucleotide sequence and expression of the menB gene from Escherichia coli. J. Bacteriol. 174:50575062.
107. Smith, L. 1954. Bacterial cytochromes. Difference spectra. Arch. Biochem. Biophys. 50:299314.
108. Sone, N. 1989. Energy transducing complexes in bacterial respiratory chains. Subcell. Biochem. 14:279337.
109. Sone, N., 1990. Respiration-driven proton pumps, p. 132. In T. A. Krulwich (ed.), The Bacteria, vol. XII. Bacterial Energetics. Academic Press, Inc., New York.
110. Sone, N.,, and Y. Fujiwara. 1991. Haem O can replace haem A in the active site of cytochrome c oxidase from thermophilic bacterium PS3. FEBS Lett. 288:154158.
111. Sone, N.,, and Y. Fujiwara. 1991. Effects of aeration during growth of Bacillus stearothermophilus on proton pumping activity and change of terminal oxidases. J. Biochem. 110:111116.
112. Sone, N.,, E. Kutoh,, and K. Sato. 1990. A cytochrome o-type oxidase of the thermophilic bacterium PS3 grown under air-limited conditions. J. Biochem. 107: 597602.
113. Sone, N.,, M. Sekimachi,, and E. Kutoh. 1987. Identification and properties of a quinol oxidase super-complex composed of a be 1 complex and cytochrome oxidase in the thermophilic bacterium PS3. J. Biol. Chem. 262:1538615391.
114. Sone, N.,, S. Shimada,, T. Ohmori,, Y. Souma,, M. Gonda,, and M. Ishizuka. 1990. A fourth subunit is present in cytochrome c oxidase from the thermophilic bacterium PS3. FEBS Lett. 262:249252.
115. Sone, N.,, and T. Takagi. 1990. Monomer-dimer structure of cytochrome c oxidase and cytochrome fee, complex from the thermophilic bacterium PS3. Biochim. Biophys. Acta 1020:207212.
116. Sone, N.,, and Y. Yanagita. 1982. A cytochrome aa3-type terminal oxidase of a thermophilic bacterium. Purification, properties and proton pumping. Biochim. Biophys. Acta 682:216226.
117. Sone, N.,, F. Yokoi,, T. Fu,, S. Ohta,, T. Metso,, M. Raitio,, and M. Saraste. 1988. Nucleotide sequence of the gene coding for cytochrome oxidase subunit I from the thermophilic bacterium PS3. J. Biochem. 103:606610.
118. Sonenshein, A. L., 1989. Metabolic regulation of sporulation and other stationary-phase phenomena, p. 109129. In I. Smith,, R. A. Slepecky,, and P. Setlow (ed.), Regulation of Procaryotic Development. American Society for Microbiology, Washington, D.C.
119. Staal, S. P.,, and J. A. Hoch. 1972. Conditional dihydro-streptomycin resistance in Bacillus subtilis. J. Bacteriol. 110:202207.
120. Taber, H. 1974. Isolation and properties of cytochrome a deficient mutants of Bacillus subtilis. J. Gen. Microbiol. 81:435444.
121. Taber, H., 1980. Functions of vitamin K2 in microorganisms, p. 177187. In J. W. Suttie (ed.), Vitamin K Metabolism and Vitamin K-Dependent Proteins. University Park Press, Baltimore, Md.
122. Taber, H.,, S. K. Farrand,, and G. M. Halfenger,. 1972. Genetic regulation of membrane components in Bacillus subtilis, p. 140147. In H. O. Halvorson,, R. S. Hanson,, and L. L. Campbell (ed.), Spores V. American Society for Microbiology, Washington, D.C.
123. Taber, H.,, and E. Freese. 1974. Sporulation properties of cytochrome a-deficient mutants of Bacillus subtilis. J. Bacteriol. 120:10041011.
124. Taber, H.,, and G. M. Halfenger. 1976. Multiple amino-glycoside-resistant mutants of Bacillus subtilis deficient in accumulation of kanamycin. Antimicrob. Agents Chemother. 9:251259.
125. Taber, H. W.,, E. A. Dellers,, and L. R. Lombarde. 1981. Menaquinone biosynthesis in Bacillus subtilis: isolation of men mutants and evidence for clustering of men genes. J. Bacteriol. 145:321327.
126. Taber, H. W.,, J. P. Mueller,, P. F. Miller,, and A. S. Arrow. 1987. Bacterial uptake of aminoglycoside antibiotics. Microbiol. Rev. 51:439457.
127. Taber, H. W.,, B. J. Sugarman,, and G. M. Halfenger. 1981. Involvement of menaquinone in active accumulation of gentamicin by Bacillus subtilis. J. Gen. Microbiol. 123:143149.
128. Takahashl, I.,, and K. Ogura. 1982. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. 92:15271537.
129. Tochikubo, K. 1971. Changes in terminal respiratory pathways of Bacillus subtilis during germination, outgrowth, and vegetative growth. J. Bacteriol. 108:652661.
130. Unden, G. 1988. Differential roles for menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their /nr-independent expression. Arch. Microbiol. 150:499503.
131. van der Oost, J.,, C. von Wachenfeld,, L. Hederstedt,, and M. Saraste. 1991. Bacillus subtilis cytochrome oxidase mutants: biochemical analysis and genetic evidence for two ao3-type oxidases. Mol. Microbiol. 5:20632072.
132. van't Rlet, J.,, F. B. Wientjes,, J. Van Doorn,, and R. J. Planta. 1979. Purification and characterization of the respiratory nitrate reductase of Bacillus licheniformis. Biochim. Biophys. Acta 576:347360.
133. von Wachenfeldt, C.,, and L. Hederstedt. 1990. Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists of a membrane-anchor and a heme domain. J. Biol. Chem. 265:1393913948.
134. von Wachenfeldt, C.,, and L. Hederstedt. 1990. Bacillus subtilis holo-cytochrome c-550 can be synthesized in aerobic Escherichia coli. FEBS Lett. 270:147151.
135. Wallace, B. J.,, and I. G. Young. 1977. Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA~ menA' double quinone mutant. Biochim. Biophys. Acta 461:84100.
136. Weber, M. M.,, and D. A. Broadbent,. 1975. Electron transport in membranes from spores and from vegetative and mother cells of Bacillus subtilis, p. 411417. In P. Gerhardt,, R. N. Costilow,, and H. L. Sadoff (ed.), Spores VI. American Society for Microbiology, Washington, D.C.
137. Wissenbach, U.,, A. Kröger,, and G. Unden. 1990. The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethyl-sulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli. Arch. Microbiol. 154:6066.
138. Wooley, K. J. 1987. The c-type cytochromes of the Gram-positive bacterium Bacillus licheniformis. Arch. Biochem. Biophys. 254:376379.
139. Yoshlda, T.,, and J. A. Fee. 1984. Studies on cytochrome c oxidase activity of thé c1aa3 complex from Thermus thermophilus. J. Biol. Chem. 259:10311036.
140. Zimmermann, B. H.,, C. I. Nitsche,, J. A. Fee,, F. Rusnak,, and E. Munck. 1988. Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus. Proc. Natl. Acad. Sci. USA 85:57795783.

Tables

Generic image for table
Table 1

Terminal oxidases identified in spp. and several other bacterial species

Citation: Taber H. 1993. Respiratory Chains, p 199-212. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch14

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