The aerobic and anaerobic respiratory chain of Escherichia coli and Salmonella enterica: Enzymes and energetics

EcoSal Plus

Volumn 3, Issue 1, 2008, Pages

  Unden, Gottfried ^a   Dünnwald, Pia ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84906232608     PISSN: None     EISSN: 23246200     Source Type: Journal    
DOI: 10.1128/ecosalplus.3.2.2     Document Type: Article

References (240)

1. Gennis RB, Stewart V. 1996. Respiration, p 217-261. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed., vol. 1. ASM Press, Washington, DC.
2. Unden G, Bongaerts J. 1997. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta 1320:217-234.
3. Schagger H. 2002. Respiratory chain supercomplexes of mitochondria and bacteria. Biochim Biophys Acta 1555:154-159.
4. Stroh A, Anderka O, Pfeiffer K, Yagi T, Finel M, Ludwig B, Schagger H. 2004. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J Biol Chem 279:5000-5007.
5. Boiangiu CD, Jayamani E, Brugel D, Herrmann G, Kim J, Forzi L, Hedderich R, Vgenopoulou I, Pierik AJ, Steuber J, Buckel W. 2005. Sodium ion pumps and hydrogen production in glutamate fermenting anaerobic bacteria. J Mol Microbiol Biotechnol 10:105-119.
6. Hussain H, Grove J, Griffiths L, Busby S, Cole J. 1994. A sevengene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria. Mol Microbiol 12:153-163.
7. Skibinski DA, Golby P, Chang YS, Sargent F, Hoffman R, Harper R, Guest JR, Attwood MM, Berks BC, Andrews SC. 2002. Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR. J Bacteriol 184:6642-6653.
8. Freedberg WB, Lin EC. 1973. Three kinds of controls affecting the expression of the glp regulon in Escherichia coli. J Bacteriol 115:816-823.
9. Yamamoto I, Ishimoto M. 1975. Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. J Biochem (Tokyo) 78:307-315.
10. Brandt U, Trumpower B. 1994. The protonmotive Q cycle in mitochondria and bacteria. Crit Rev Biochem Mol Biol 29:165-197.
11. Hunte C, Palsdottir H, Trumpower BL. 2003. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett 545:39-46.
12. Mitchell P. 1979. Keilin's respiratory chain concept and its chemiosmotic consequences. Science 206:1148-1159.
13. Friedrich T. 1998. The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim Biophys Acta 1364:134-146.
14. Guenebaut V, Schlitt A, Weiss H, Leonard K, Friedrich T. 1998. Consistent structure between bacterial and mitochondrial NADH: ubiquinone oxidoreductase (complex I). J Mol Biol 276:105-112.
15. Leif H, Weidner U, Berger A, Spehr V, Braun M, van Heek P, Friedrich T, Ohnishi T, Weiss H. 1993. Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I. Biochem Soc Trans 21:998-1001.
16. Weidner U, Geier S, Ptock A, Friedrich T, Leif H, Weiss H. 1993. The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J Mol Biol 233:109-122.
17. Yagi T, Yano T, Matsuno-Yagi A. 1993. Characteristics of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches. J Bioenerg Biomembr 25:339-345.
18. Bongaerts J, Zoske S, Weidner U, Unden G. 1995. Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors and gene regulators. Mol Microbiol 16:521-534.
19. Calhoun MW, Gennis RB. 1993. Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. J Bacteriol 175:3013-3019.
20. Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. 1993. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol 175:3020-3025.
21. Tran QH, Bongaerts J, Vlad D, Unden G. 1997. Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur J Biochem 244:155-160.
22. Sazanov LA, Hinchliffe P. 2006. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311:1430-1436.
23. Holt PJ, Morgan DJ, Sazanov LA. 2003. The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping. J Biol Chem 278:43114-43120.
24. Kao MC, Di Bernardo S, Perego M, Nakamaru-Ogiso E, Matsuno-Yagi A, Yagi T. 2004. Functional roles of four conserved charged residues in the membrane domain subunit NuoA of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. J Biol Chem 279:32360-32366.
25. Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T. 1995. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem 230:538-548.
26. Stolpe S, Friedrich T. 2004. The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport. J Biol Chem 279:18377-18783.
27. Steuber J. 2003. The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+. J Biol Chem 278:26817-26822.
28. Steuber J, Schmid C, Rufibach M, Dimroth P. 2000. Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli. Mol Microbiol 35:428-434.
29. Berg BL, Stewart V. 1990. Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics 125:691-702.
30. Darwin A, Tormay P, Page L, Griffiths L, Cole J. 1993. Identification of the formate dehydrogenases and genetic determinants of formate-dependent nitrite reduction by Escherichia coli K12. J Gen Microbiol 139:1829-1840.
31. Enoch HG, Lester RL. 1975. The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. J Biol Chem 250:6693-6705.
32. Li J, Stewart V. 1992. Localization of upstream sequence elements required for nitrate and anaerobic induction of fdn (formate dehydrogenase-N) operon expression in Escherichia coli K-12. J Bacteriol 174:4935-4942.
33. Jormakka M, Byrne B, Iwata S. 2003. Protonmotive force generation by a redox loop mechanism. FEBS Lett 545:25-30.
34. Jormakka M, Tornroth S, Byrne B, Iwata S. 2002. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295:1863-1868.
35. Jones RW. 1980. Proton translocation by the membrane-bound formate dehydrogenase of Escherichia coli. FEMS Microbiol Lett 8:167-171.
36. Abaibou H, Pommier J, Benoit S, Giordano G, Mandrand-Berthelot MA. 1995. Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. J Bacteriol 177:7141-7149.
37. Pommier J, Mandrand MA, Holt SE, Boxer DH, Giordano G. 1992. A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli. Biochim Biophys Acta 1107:305-513.
38. Benoit S, Abaibou H, Mandrand-Berthelot MA. 1998. Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli. J Bacteriol 180:6625-6634.
39. Stanley NR, Sargent F, Buchanan G, Shi J, Stewart V, Palmer T, Berks BC. 2002. Behaviour of topological marker proteins targeted to the Tat protein transport pathway. Mol Microbiol 43:1005-1021.
40. Böck A, King PW, Blokesch M, Posewitz MC. 2006. Maturation of hydrogenases. Adv Microb Physiol 51:1-71.
41. Dross F, Geisler V, Lenger R, Theis F, Krafft T, Fahrenholz F, Kojro E, Duchene A, Tripier D, Juvenal K. 1992. The quinonereactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur J Biochem 206:93-102.
42. Gross R, Pisa R, Sanger M, Lancaster CR, Simon J. 2004. Characterization of the menaquinone reduction site in the diheme cytochrome b membrane anchor of Wolinella succinogenes NiFehydrogenase. J Biol Chem 279:274-281.
43. Gross R, Simon J, Lancaster CR, Kröger A. 1998. Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2. Mol Microbiol 30:639-646.
44. Gross R, Simon J, Theis F, Kröger A. 1998. Two membrane anchors of Wolinella succinogenes hydrogenase and their function in fumarate and polysulfide respiration. Arch Microbiol 170: 50-58.
45. Unden G, Bocher R, Knecht J, Kröger A. 1982. Hydrogenase from Vibrio succinogenes, a nickel protein. FEBS Lett 145:230-234.
46. Menon NK, Chatelus CY, Dervartanian M, Wendt JC, Shanmugam KT, Peck HD, Jr, Przybyla AE. 1994. Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2. J Bacteriol 176:4416-4423.
47. Menon NK, Robbins J, Peck HD, Jr, Chatelus CY, Choi ES, Przybyla AE. 1990. Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames. J Bacteriol 172:1969-1977.
48. Richard DJ, Sawers G, Sargent F, McWalter L, Boxer DH. 1999. Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli. Microbiology 145(Pt 10):2903-2912.
49. Sawers G. 1994. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66:57-88.
50. Sawers RG, Ballantine SP, Boxer DH. 1985. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J Bacteriol 164:1324-1331.
51. Sawers RG, Boxer DH. 1986. Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12. Eur J Biochem 156:265-275.
52. Gross R, Simon J, Kröger A. 1999. The role of the twinarginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from Wolinella succinogenes. Arch Microbiol 172:227-232.
53. Kröger A, Biel S, Simon J, Gross R, Unden G, Lancaster CR. 2002. Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism. Biochim Biophys Acta 1553:23-38.
54. Ballantine SP, Boxer DH. 1986. Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli. Eur J Biochem 156:277-284.
55. Dubini A, Pye RL, Jack RL, Palmer T, Sargent F. 2002. How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli. Int J Hydrogen Energy 27:1413-1420.
56. Sargent F, Ballantine SP, Rugman PA, Palmer T, Boxer DH. 1998. Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit-identification of a soluble precursor of the small subunit in a hypB mutant. Eur J Biochem 255:746-754.
57. Bernhard T, Gottschalk G. 1978. Cell yields of Escherichia coli during anaerobic growth on fumarate and molecular hydrogen. Arch Microbiol 116:235-238.
58. Laurinavichene TV, Tsygankov AA. 2001. H2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors. FEMS Microbiol Lett 202:121-124.
59. Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S. 2003. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science 299:700-704.
60. Cecchini G, Schroder I, Gunsalus RP, Maklashina E. 2002. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim Biophys Acta 1553:140-157.
61. Lancaster CR. 2002. Succinate:quinone oxidoreductases: an overview. Biochim Biophys Acta 1553:1-6.
62. Tornroth S, Yankovskaya V, Cecchini G, Iwata S. 2002. Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli. Biochim Biophys Acta 1553:171-176.
63. Schirawski J, Unden G. 1998. Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential. Eur J Biochem 257:210-215.
64. Zaunmuller T, Kelly DJ, Glockner FO, Unden G. 2006. Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria. Microbiology 152:2443-2453.
65. Hagerhall C, Hederstedt L. 1996. A structural model for the membrane-integral domain of succinate:quinone oxidoreductases. FEBS Lett 389:25-31.
66. Schnorpfeil M, Janausch IG, Biel S, Kröger A, Unden G. 2001. Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase. Eur J Biochem 268:3069-3074.
67. Ameyama M, Nonobe M, Shinagawa E, Matsushita K, Takimoto K, Adachi O. 1986. Purification and characterization of the quinoprotein D-glucose dehydrogenase apoenzyme from Escherichia coli. Agric Biol Chem 50:49-57.
68. Hommes RJW, Postma PW, Neijssel OM, Tempest DW, Dokter P, Duine JA. 1984. Evidence of a quinoprotein glucose dehydrogenase apoenzyme in several strains of Escherichia coli. FEMS Microbiol Lett 24:329-333.
69. Yamada M, Asaoka S, Saier MH, Jr, Yamada Y. 1993. Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression. J Bacteriol 175:568-571.
70. Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y. 1993. Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site. J Biol Chem 268:12812-12817.
71. Cozier GE, Anthony C. 1995. Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem J 312(Pt 3):679-685.
72. van Schie BJ, Hellingwerf KJ, van Dijken JP, Elferink MG, van Dijl JM, Kuenen JG, Konings WN. 1985. Energy transduction by electron transfer via a pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus (var. lwoffi). J Bacteriol 163:493-499.
73. Yamada M, Elias MD, Matsushita K, Migita CT, Adachi O. 2003. Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoproteins. Biochim Biophys Acta 1647:185-192.
74. Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada M. 2001. C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone. J Biol Chem 276:48356-48361.
75. Friedrich T, Strohdeicher M, Hofhaus G, Preis D, Sahm H, Weiss H. 1990. The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase. FEBS Lett 265:37-40.
76. Campbell HD, Rogers BL, Young IG. 1984. Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of Escherichia coli. Eur J Biochem 144:367-373.
77. Kaczorowski G, Kohn LD, Kaback HR. 1978. Purification and properties of D-lactate dehydrogenase from Escherichia coli ML 308-225. Methods Enzymol 53:519-527.
78. Matsushita K, Kaback HR. 1986. D-Lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry 25:2321-2327.
79. Rule GS, Pratt EA, Chin CC, Wold F, Ho C. 1985. Overproduction and nucleotide sequence of the respiratory D-lactate dehydrogenase of Escherichia coli. J Bacteriol 161:1059-1068.
80. Tanaka Y, Anraku Y, Futai M. 1976. Escherichia coli membrane D-lactate dehydrogenase. Isolation of the enzyme in aggregated from and its activation by Triton X-100 and phospholipids. J Biochem (Tokyo) 80:821-830.
81. Dym O, Pratt EA, Ho C, Eisenberg D. 2000. The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc Natl Acad Sci USA 97:9413-9418.
82. Sun ZY, Truong HT, Pratt EA, Sutherland DC, Kulig CE, Homer RJ, Groetsch SM, Hsue PY, Ho C. 1993. A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli. Protein Sci 2:1938-1947.
83. Chang YY, Cronan JE, Jr. 1983. Genetic and biochemical analyses of Escherichia coli strains having a mutation in the structural gene (poxB) for pyruvate oxidase. J Bacteriol 154:756-762.
84. Gennis RB, Hager LP. 1976. Pyruvate oxidase, p 493-504. In Martinosi A (ed), The Enzymes of Biological Membranes, vol. 2. Plenum Publishing Corp., New York, NY.
85. Grabau C, Cronan JE, Jr. 1986. Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipidactivated flavoprotein. Nucleic Acids Res 14:5449-5460.
86. Wang AY, Chang YY, Cronan JE, Jr. 1991. Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding. J Biol Chem 266:10959-10966.
87. Chang YY, Cronan JE. 1984. An Escherichia coli mutant deficient in pyruvate oxidase activity due to altered phospholipid activation of the enzyme. Proc Natl Acad Sci USA 81:4348-4352.
88. Chang YY, Cronan JE, Jr. 1995. Detection by site-specific disulfide cross-linking of a conformational change in binding of Escherichia coli pyruvate oxidase to lipid bilayers. J Biol Chem 270: 7896-7901.
89. Chang YY, Cronan JE, Jr. 1997. Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase. Biochemistry 36:11564-11573.
90. Carter K, Gennis RB. 1985. Reconstitution of the ubiquinonedependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex. J Biol Chem 260:10986-10990.
91. Koland JG, Miller MJ, Gennis RB. 1984. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry 23:445-453.
92. Jaworowski A, Campbell HD, Poulis MI, Young IG. 1981. Genetic identification and purification of the respiratory NADH dehydrogenase of Escherichia coli. Biochemistry 20:2041-2047.
93. Jaworowski A, Mayo G, Shaw DC, Campbell HD, Young IG. 1981. Characterization of the respiratory NADH dehydrogenase of Escherichia coli and reconstitution of NADH oxidase in ndh mutant membrane vesicles. Biochemistry 20:3621-3628.
94. Matsushita K, Ohnishi T, Kaback HR. 1987. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26:7732-7737.
95. Spiro S, Roberts RE, Guest JR. 1989. FNR-dependent repression of the ndh gene of Escherichia coli and metal ion requirement for FNR-regulated gene expression. Mol Microbiol 3:601-608.
96. Bjorklof K, Zickermann V, Finel M. 2000. Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues. FEBS Lett 467:105-110.
97. Narindrasorasak S, Goldie AH, Sanwal BD. 1979. Characteristics and regulation of a phospholipid-activated malate oxidase from Escherichia coli. J Biol Chem 254:1540-1545.
98. van der Rest ME, Frank C, Molenaar D. 2000. Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli. J Bacteriol 182:6892-6899.
99. Molenaar D, van der Rest ME, Petrovic S. 1998. Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum. Eur J Biochem 254:395-403.
100. Dong JM, Taylor JS, Latour DJ, Iuchi S, Lin EC. 1993. Three overlapping lct genes involved in L-lactate utilization by Escherichia coli. J Bacteriol 175:6671-6678.
101. Futai M, Kimura H. 1977. Inducible membrane-bound L-lactate dehydrogenase from Escherichia coli. Purification and properties. J Biol Chem 252:5820-5827.
102. Iuchi S, Aristarkhov A, Dong JM, Taylor JS, Lin EC. 1994. Effects of nitrate respiration on expression of the Arc-controlled operons encoding succinate dehydrogenase and flavin-linked L-lactate dehydrogenase. J Bacteriol 176:1695-1701.
103. Kimura H, Futai M. 1978. Effects of phospholipids on L-lactate dehydrogenase from membranes of Escherichia coli. Activation and stabilization of the enzyme with phospholipids. J Biol Chem 253: 1095-1110.
104. Austin D, Larson TJ. 1991. Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12. J Bacteriol 173:101-107.
105. Schweizer H, Larson TJ. 1987. Cloning and characterization of the aerobic sn-glycerol-3-phosphate dehydrogenase structural gene glpD of Escherichia coli K-12. J Bacteriol 169:507-513.
106. Walz AC, Demel RA, de Kruijff B, Mutzel R. 2002. Aerobic snglycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix. Biochem J 365:471-479.
107. Janes BK, Bender RA. 1998. Alanine catabolism in Klebsiella aerogenes: molecular characterization of the dadAB operon and its regulation by the nitrogen assimilation control protein. J Bacteriol 180:563-570.
108. Lobocka M, Hennig J, Wild J, Klopotowski T. 1994. Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of D-amino acid dehydrogenase and the catabolic alanine racemase. J Bacteriol 176:1500-1510.
109. Olsiewski PJ, Kaczorowski GJ, Walsh C. 1980. Purification and properties of D-amino acid dehydrogenase, an inducible membranebound iron-sulfur flavoenzyme from Escherichia coli B. J Biol Chem 255:4487-4494.
110. Jones H, Venables WA. 1983. Effects of solubilisation on some properties of the membrane-bound respiratory enzyme D-amino acid dehydrogenase of Escherichia coli. FEBS Lett 151:189-192.
111. Cole ST, Eiglmeier K, Ahmed S, Honore N, Elmes L, Anderson WF, Weiner JH. 1988. Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic snglycerol-3-phosphate dehydrogenase of Escherichia coli K-12. J Bacteriol 170:2448-2456.
112. Iuchi S, Cole ST, Lin EC. 1990. Multiple regulatory elements for the glpA operon encoding anaerobic glycerol-3-phosphate dehydrogenase and the glpD operon encoding aerobic glycerol-3-phosphate dehydrogenase in Escherichia coli: further characterization of respiratory control. J Bacteriol 172:179-184.
113. Kistler WS, Lin EC. 1971. Anaerobic L-α-glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role. J Bacteriol 108:1224-1234.
114. Kuritzkes DR, Zhang XY, Lin EC. 1984. Use of phi(glp-lac) in studies of respiratory regulation of the Escherichia coli anaerobic snglycerol-3-phosphate dehydrogenase genes (glpAB). J Bacteriol 157: 591-598.
115. Varga ME, Weiner JH. 1995. Physiological role of GlpB of anaerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. Biochem Cell Biol 73:147-153.
116. Schryvers A, Weiner JH. 1981. The anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli. Purification and characterization. J Biol Chem 256:9959-9965.
117. Thauer RK, Jungermann K, Decker K. 1977. Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41:100-180.
118. Tran QH, Unden G. 1998. Changes in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation. Eur J Biochem 251:538-543.
119. Leonhartsberger S, Korsa I, Böck A. 2002. The molecular biology of formate metabolism in enterobacteria. J Mol Microbiol Biotechnol 4:269-276.
120. Sawers G, Blokesch M, Böck A. 9 September 2004, posting date. Anaerobic Formate and Hydrogen Metabolism, Anaerobic Formate and Hydrogen Metabolism. In Böck A, Curtiss R III, Kaper JB, Karp PD, Neidhardt FC, Nyström T, Slauch JM, and Squires CL (ed), EcoSal-Escherichia and Salmonella: cellular and molecular biology. http://www.ecosal.org. ASM Press, Washington, DC.
121. Koo MS, Lee JH, Rah SY, Yeo WS, Lee JW, Lee KL, Koh YS, Kang SO, Roe JH. 2003. A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J 22:2614-2622.
122. Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR. 1997. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143(Pt 11):3633-3647.
123. Self WT, Hasona A, Shanmugam KT. 2004. Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli. J Bacteriol 186:580-587.
124. Storz G, Imlay JA. 1999. Oxidative stress. Curr Opin Microbiol 2:188-194.
125. Kobayashi K, Tagawa S. 1999. Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli. FEBS Lett 451:227-230.
126. Jouanneau Y, Jeong HS, Hugo N, Meyer C, Willison JC. 1998. Overexpression in Escherichia coli of the rnf genes from Rhodobacter capsulatus-characterization of two membrane-bound iron-sulfur proteins. Eur J Biochem 251:54-64.
127. Kumagai H, Fujiwara T, Matsubara H, Saeki K. 1997. Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH oxidoreductases. Biochemistry 36:5509-5521.
128. Schmehl M, Jahn A, Meyer zu Vilsendorf A, Hennecke S, Masepohl B, Schuppler M, Marxer M, Oelze J, Klipp W. 1993. Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. Mol Gen Genet 241:602-615.
129. Ding H, Hidalgo E, Demple B. 1996. The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J Biol Chem 271:33173-33175.
130. Andrews S, Cox GB, Gibson F. 1977. The anaerobic oxidation of dihydroorotate by Escherichia coli K-12. Biochim Biophys Acta 462:153-160.
131. Karibian D. 1978. Dihydroorotate dehydrogenase (Escherichia coli). Methods Enzymol 51:58-63.
132. Karibian D, Couchoud P. 1974. Dihydro-orotate oxidase of Escherichia coli K12: purification, properties, and relation to the cytoplasmic membrane. Biochim Biophys Acta 364:218-232.
133. Larsen JN, Jensen KF. 1985. Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase. Eur J Biochem 151:59-65.
134. Nørager S, Jensen KF, Björnberg O, Larsen S. 2002. E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure 10:1211-1223.
135. Bader M, Muse W, Ballou DP, C Gassner, Bardwell J. 1999. Oxidative protein folding is driven by the electron transport system. Cell 98:217-227.
136. Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, Ito K. 2006. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127:789-801.
137. Malpica R, Franco B, Rodriguez C, Kwon O, Georgellis D. 2004. Identification of a quinone-sensitive redox switch in the ArcB sensor kinase. Proc Natl Acad Sci USA 101:13318-13323.
138. Jacobs NJ, Jacobs JM. 1978. Quinones as hydrogen carriers for a late step in anaerobic heme biosynthesis in Escherichia coli. Biochim Biophys Acta 544:540-546.
139. Nishimura K, Nakayashiki T, Inokuchi H. 1995. Cloning and identification of the hemG gene encoding protoporphyrinogen oxidase (PPO) of Escherichia coli K-12. DNA Res 2:1-8.
140. Dailey HA (ed). 1990. Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: terminal three enzymes, p 123-161. In Biosynthesis of Heme and Chlorophylls. McGraw Hill, New York, NY.
141. Wikstrom M, Jasaitis A, Backgren C, Puustinen A, Verkhovsky MI. 2000. The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases. Biochim Biophys Acta 1459:514-520.
142. Cotter PA, Gunsalus RP. 1992. Contribution of the fnr and arcA gene products in coordinate regulation of cytochrome o and d oxidase (cyoABCDE and cydAB) genes in Escherichia coli. FEMS Microbiol Lett 70:31-36.
143. Lanciano P, Vergnes A, Grimaldi S, Guigliarelli B, Magalon A. 2007. Biogenesis of a respiratory complex is orchestrated by a single accessory protein. J Biol Chem 282:17468-17474.
144. Liu X, DeMoss JA. 1997. Characterization of NarJ, a systemspecific chaperone required for nitrate reductase biogenesis in Escherichia coli. J Biol Chem 272:24266-24271.
145. Stewart V. 2003. Biochemical Society Special Lecture. Nitrateand nitrite-responsive sensors NarX and NarQ of proteobacteria. Biochem Soc Trans 31:1-10.
146. Bonnefoy V, Demoss JA. 1994. Nitrate reductases in Escherichia coli. Antonie Van Leeuwenhoek 66:47-56.
147. Berks BC, Page MD, Richardson DJ, Reilly A, Cavill A, Outen F, Ferguson SJ. 1995. Sequence analysis of subunits of the membranebound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electroncarrying arm of a redox loop. Mol Microbiol 15:319-331.
148. Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC. 2003. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat Struct Biol 10:681-687.
149. Page CC, Moser CC, Chen X, Dutton PL. 1999. Natural engineering principles of electron tunnelling in biological oxidationreduction. Nature 402:47-52.
150. Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC. 2005. Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. J Biol Chem 280:14836-14843.
151. Rothery RA, Blasco F, Magalon A, Weiner JH. 2001. The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols. J Mol Microbiol Biotechnol 3:273-283.
152. Zhao Z, Rothery RA, Weiner JH. 2003. Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol. Biochemistry 42:5403-5413.
153. Zhao Z, Weiner JH. 1998. Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli. J Biol Chem 273:20758-20763.
154. Blasco F, Iobbi C, Ratouchniak J, Bonnefoy V, Chippaux M. 1990. Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. Mol Gen Genet 222:104-111.
155. Iobbi-Nivol C, Santini CL, Blasco F, Giordano G. 1990. Purification and further characterization of the second nitrate reductase of Escherichia coli K12. Eur J Biochem 188:679-687.
156. Chang L, Wei LI, Audia JP, Morton RA, Schellhorn HE. 1999. Expression of the Escherichia coli NRZ nitrate reductase is highly growth phase dependent and is controlled by RpoS, the alternative vegetative sigma factor. Mol Microbiol 34:756-766.
157. Spector MP, Garcia del Portillo F, Bearson SM, Mahmud A, Magut M, Finlay BB, Dougan G, Foster JW, Pallen MJ. 1999. The rpoS-dependent starvation-stress response locus stiA encodes a nitrate reductase (narZYWV) required for carbon-starvation-inducible thermotolerance and acid tolerance in Salmonella typhimurium. Microbiology 145(Pt 11):3035-3045.
158. Kita K, Konishi K, Anraku Y. 1986. Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain. Methods Enzymol 126:94-113.
159. Miller MJ, Gennis RB. 1985. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J Biol Chem 260:14003-14008.
160. Miller MJ, Gennis RB. 1983. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem 258:9159-9165.
161. Govantes F, Albrecht JA, Gunsalus RP. 2000. Oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operon: roles of multiple promoters and the Fnr-1 and Fnr-2 binding sites. Mol Microbiol 37:1456-1469.
162. Iuchi S, Lin EC. 1991. Adaptation of Escherichia coli to respiratory conditions: regulation of gene expression. Cell 66:5-7.
163. Trumpower BL, Gennis RB. 1994. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation. Annu Rev Biochem 63:675-716.
164. Dassa J, Fsihi H, Marck C, Dion M, Kieffer-Bontemps M, Boquet PL. 1991. A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA). Mol Gen Genet 229:341-352.
165. Sturr MG, Krulwich TA, Hicks DB. 1996. Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4. J Bacteriol 178:1742-1749.
166. Cole ST, Condon C, Lemire BD, Weiner JH. 1985. Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli. Biochim Biophys Acta 811:381-403.
167. Hirsch CA, Rasminsky M, Davis BD, Lin EC. 1963. A fumarate reductase in Escherichia coli distinct from succinate dehydrogenase. J Biol Chem 238:3770-3774.
168. Unden G, Kleefeld A. 30 July 2004, posting date. C4-Dicarboxylate Degradation in Aerobic and Anaerobic Growth, C4-Dicarboxylate Degradation in Aerobic and Anaerobic Growth. In Böck A, Curtiss R III, Kaper JB, Karp PD, Neidhardt FC, Nyström T, Slauch JM, and Squires CL (ed), EcoSal-Escherichia and Salmonella: cellular and molecular biology. http://www.ecosal.org. ASM Press, Washington, DC.
169. Kröger A. 1974. Electron-transport phosphorylation coupled to fumarate reduction in anaerobically grown Proteus rettgeri. Biochim Biophys Acta 347:273-289.
170. Engel P, Krämer R, Unden G. 1994. Transport of C4-dicarboxylates by anaerobically grown Escherichia coli. Energetics and mechanism of exchange, uptake and efflux. Eur J Biochem 222:605-614.
171. Janausch IG, Zientz E, Tran QH, Kröger A, Unden G. 2002. C4-dicarboxylate carriers and sensors in bacteria. Biochim Biophys Acta 1553:39-56.
172. Six S, Andrews SC, Unden G, Guest JR. 1994. Escherichia coli possesses two homologous anaerobic C4-dicarboxylate membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate transport system (Dct). J Bacteriol 176:6470-6478.
173. Zientz E, Six S, Unden G. 1996. Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the three Dcu carriers in uptake and exchange. J Bacteriol 178:7241-7247.
174. Dickie P, Weiner JH. 1979. Purification and characterization of membrane-bound fumarate reductase from anaerobically grown Escherichia coli. Can J Biochem 57:813-821.
175. Iverson TM, Luna-Chavez C, Cecchini G, Rees DC. 1999. Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284:1961-1966.
176. McCrindle SL, Kappler U, McEwan AG. 2005. Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration. Adv Microb Physiol 50:147-198.
177. McEwan AG, Ridge JP, McDevitt CA, Hugenholtz P. 2002. The DMSO reductase family of microbial molybdenum enzymes; molecular properties and role of the dissimilatory reduction of toxic elements. Geomicrobiol J 19:3-21.
178. Berks BC. 1996. A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22:393-404.
179. Rothery RA, Weiner JH. 1993. Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster. Biochemistry 32:5855-5861.
180. Weiner JH, Shaw G, Turner RJ, Trieber CA. 1993. The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli. J Biol Chem 268:3238-3244.
181. Geijer P, Weiner JH. 2004. Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli. Biochim Biophys Acta 1660:66-74.
182. Sambasivarao D, Weiner JH. 1991. Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation. J Bacteriol 173:5935-5943.
183. Lubitz SP, Weiner JH. 2003. The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC). Arch Biochem Biophys 418:205-216.
184. Mejean V, Iobbi-Nivol C, Lepelletier M, Giordano G, Chippaux M, Pascal MC. 1994. TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon. Mol Microbiol 11: 1169-1179.
185. Genest O, Ilbert M, Mejean V, Iobbi-Nivol C. 2005. TorD, an essential chaperone for TorA molybdoenzyme maturation at high temperature. J Biol Chem 280:15644-15648.
186. Ilbert M, Mejean V, Giudici-Orticoni MT, Samama JP, Iobbi-Nivol C. 2003. Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA. J Biol Chem 278:28787-28792.
187. Gon S, Giudici-Orticoni MT, Mejean V, Iobbi-Nivol C. 2001. Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J Biol Chem 276:11545-11551.
188. Pascal MC, Burini JF, Chippaux M. 1984. Regulation of the trimethylamine N-oxide (TMAO) reductase in Escherichia coli: analysis of tor::Mud1 operon fusion. Mol Gen Genet 195:351-355.
189. Baraquet C, Theraulaz L, Guiral M, Lafitte D, Mejean V, Jourlin-Castelli C. 2006. TorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli. J Biol Chem 281:38189-38199.
190. Jourlin C, Bengrine A, Chippaux M, Mejean V. 1996. An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli. Mol Microbiol 20:1297-1306.
191. Gon S, Patte JC, Mejean V, Iobbi-Nivol C. 2000. The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine Noxide reductase in Escherichia coli. J Bacteriol 182:5779-5786.
192. Richardson DJ, Berks BC, Russell DA, Spiro S, Taylor CJ. 2001. Functional, biochemical and genetic diversity of prokaryotic nitrate reductases. Cell Mol Life Sci 58:165-178.
193. Stewart V, Lu Y, Darwin AJ. 2002. Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12. J Bacteriol 184:1314-1323.
194. Potter LC, Millington P, Griffiths L, Thomas GH, Cole JA. 1999. Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth? Biochem J 344(Pt 1):77-84.
195. Wang H, Tseng CP, Gunsalus RP. 1999. The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite. J Bacteriol 181:5303-5308.
196. Brondijk TH, Fiegen D, Richardson DJ, Cole JA. 2002. Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation. Mol Microbiol 44:245-255.
197. Nilavongse A, Brondijk TH, Overton TW, Richardson DJ, Leach ER, Cole JA. 2006. The NapF protein of the Escherichia coli periplasmic nitrate reductase system: demonstration of a cytoplasmic location and interaction with the catalytic subunit, NapA. Microbiology 152:3227-3237.
198. Olmo-Mira MF, Gavira M, Richardson DJ, Castillo F, Moreno-Vivian C, Roldan MD. 2004. NapF is a cytoplasmic iron-sulfur protein required for Fe-S cluster assembly in the periplasmic nitrate reductase. J Biol Chem 279:49727-49735.
199. Brondijk TH, Nilavongse A, Filenko N, Richardson DJ, Cole JA. 2004. NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing. Biochem J 379:47-55.
200. Simon J. 2002. Enzymology and bioenergetics of respiratory nitrite ammonification. FEMS Microbiol Rev 26:285-309.
201. Cole J. 1996. Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation? FEMS Microbiol Lett 136:1-11.
202. Page L, Griffiths L, Cole JA. 1990. Different physiological roles of two independent pathways for nitrite reduction to ammonia by enteric bacteria. Arch Microbiol 154:349-354.
203. Wang H, Gunsalus RP. 2000. The nrfA and nirB nitrite reductase operons in Escherichia coli are expressed differently in response to nitrate than to nitrite. J Bacteriol 182:5813-5822.
204. Jackson RH, Cornish-Bowden A, Cole JA. 1981. Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem J 193:861-867.
205. Abou-Jaoude A, Chippaux M, Pascal MC. 1979. Formate-nitrite reduction in Escherichia coli K12. 1. Physiological study of the system. Eur J Biochem 95:309-314.
206. Pope NR, Cole JA. 1982. Generation of a membrane potential by one of two independent pathways for nitrite reduction by Escherichia coli. J Gen Microbiol 128:219-222.
207. Potter L, Angove H, Richardson D, Cole J. 2001. Nitrate reduction in the periplasm of gram-negative bacteria. Adv Microb Physiol 45:51-112.
208. Fujita T. 1966. Studies on soluble cytochromes in Enterobacteriaceae. I. Detection, purification, and properties of cytochrome c-552 in anaerobically grown cells. J Biochem (Tokyo) 60: 204-215.
209. Kajie S, Anraku Y. 1986. Purification of a hexaheme cytochrome c552 from Escherichia coli K 12 and its properties as a nitrite reductase. Eur J Biochem 154:457-463.
210. Liu MC, Peck HD, Jr, Abou-Jaoudé A, Chippaux M, LeGall J. 1981. A reappraisal of the role of the low potential c-type cytochrome (cytochrome c-552) in NADH-dependent nitrite reduction and its relationship with a co-purified NADH-oxidase in Escherichia coli K-12. FEMS Microbiol Lett 10:333-337.
211. Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ. 2002. Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli. Biochemistry 41:2921-2931.
212. Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM. 1999. Structure of cytochrome c nitrite reductase. Nature 400:476-480.
213. Grovc J, Busby S, Cole J. 1996. The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli. Mol Gen Genet 252:332-341.
214. Iobbi-Nivol C, Crooke H, Griffiths L, Grove J, Hussain H, Pommier J, Mejean V, Cole JA. 1994. A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12. FEMS Microbiol Lett 119:89-94.
215. Einsle O, Stach P, Messerschmidt A, Simon J, Kröger A, Huber R, Kroneck PM. 2000. Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 Å resolution, inhibitor binding, and heme-packing motifs. J Biol Chem 275:39608-39616.
216. Simon J, Gross R, Einsle O, Kroneck PM, Kröger A, Klimmek O. 2000. A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes. Mol Microbiol 35:686-696.
217. Price-Carter M, Tingey J, Bobik TA, Roth JR. 2001. The alternative electron acceptor tetrathionate supports B12-dependent anaerobic growth of Salmonella enterica serovar typhimurium on ethanolamine or 1,2-propanediol. J Bacteriol 183:2463-2475.
218. Hensel M, Hinsley AP, Nikolaus T, Sawers G, Berks BC. 1999. The genetic basis of tetrathionate respiration in Salmonella typhimurium. Mol Microbiol 32:275-287.
219. Hinsley AP, Berks BC. 2002. Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica. Microbiology 148:3631-3638.
220. Clark MA, Barrett EL. 1987. The phs gene and hydrogen sulfide production by Salmonella typhimurium. J Bacteriol 169:2391-2397.
221. Alami N, Hallenbeck PC. 1995. Cloning and characterization of a gene cluster, phsBCDEF, necessary for the production of hydrogen sulfide from thiosulfate by Salmonella typhimurium. Gene 156:53-57.
222. Heinzinger NK, Fujimoto SY, Clark MA, Moreno MS, Barrett EL. 1995. Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism. J Bacteriol 177:2813-2820.
223. Hallenbeck PC, Clark MA, Barrett EL. 1989. Characterization of anaerobic sulfite reduction by Salmonella typhimurium and purification of the anaerobically induced sulfite reductase. J Bacteriol 171:3008-3015.
224. Meganathan R. 1996. Biosynthesis of the isoprenoid quinones menaquinone (vitamin K2) and ubiquinone (coenzyme Q), p 642-656. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. ASM Press, Washington, DC.
225. Unden G. 1988. Differential roles for menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their fnr-independent expression. Arch Microbiol 150:499-503.
226. Wallace BJ, Young IG. 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 461:84-100.
227. Collins MD, Jones D. 1981. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication. Microbiol Rev 45:316-354.
228. Guest JR, Shaw DJ. 1981. Molecular cloning of menaquinone biosynthetic genes of Escherichia coli K12. Mol Gen Genet 181:379-383.
229. Kwan HS, Barrett EL. 1983. Roles for menaquinone and the two trimethylamine oxide (TMAO) reductases in TMAO respiration in Salmonella typhimurium: Mu d(Apr lac) insertion mutations in men and tor. J Bacteriol 155:1147-1155.
230. Meganathan R. 1984. Inability of men mutants of Escherichia coli to use trimethylamine-N-oxide as an electron acceptor. FEMS Microbiol Lett 24:57-62.
231. Tyson K, Metheringham R, Griffiths L, Cole J. 1997. Characterisation of Escherichia coli K-12 mutants defective in formatedependent nitrite reduction: essential roles for hemN and the menFDBCE operon. Arch Microbiol 168:403-411.
232. Wissenbach U, Kröger A, Unden G. 1990. The specific functions of menaquinone and demethylmenaquinone in anaerobic res-piration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli. Arch Microbiol 154:60-66.
233. Wissenbach U, Ternes D, Unden G. 1992. An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration. Arch Microbiol 158:68-73.
234. Novotny C, Kapralek F. 1979. Participation of quinone and cytochrome b in tetrathionate reductase respiratory chain of Citrobacter freundii. Biochem J 178:237-240.
235. Cole HA, Wimpenny JW, Hughes DE. 1967. The ATP pool in Escherichia coli. I. Measurement of the pool using modified luciferase assay. Biochim Biophys Acta 143:445-453.
236. Hellingwerf KJ, Bolscher JG, Konings WN. 1981. The electrochemical proton gradient generated by the fumarate-reductase system in Escherichia coli and its bioenergetic implications. Eur J Biochem 113:369-374.
237. Jiang W, Hermolin J, Fillingame RH. 2001. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc Natl Acad Sci USA 98:4966-4971.
238. Meier T, Yu J, Raschle T, Henzen F, Dimroth P, Muller DJ. 2005. Structural evidence for a constant c11 ring stoichiometry in the sodium F-ATP synthase. FEBS J 272:5474-5483.
239. Kashket ER. 1983. Stoichiometry of the H+-ATPase of Escherichia coli cells during anaerobic growth. FEBS Lett 154:343-346.
240. Green J, Guest JR. 1994. Regulation of transcription at the ndh promoter of Escherichia coli by FNR and novel factors. Mol Microbiol 12:433-444.