The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1827, Issue 8-9, 2013, Pages 1048-1085

  Grimaldi, Stéphane ^a   Schoepp Cothenet, Barbara ^a   Ceccaldi, Pierre ^a,b   Guigliarelli, Bruno ^a   Magalon, Axel ^b  

^a AIX MARSEILLE UNIVERSITÉ   (France)

^b AIX MARSEILLE UNIVERSITÉ   (France)

Author keywords

Bioenergetic; Electron transfer; Iron sulfur; Molybdenum; Prokaryote; Quinone

Indexed keywords

ACETYLENE HYDRATASE; ARSENATE REDUCTASE; ARSENITE OXIDASE; C25 DEHYDROGENASE; CHLORATE REDUCTASE; CYSTEINE; DIMETHYL SULFOXIDE REDUCTASE; DITHIONITE; ETHYLBENZENE DEHYDROGENASE; FORMATE DEHYDROGENASE; METHIONINE; MOLYBDENUM; NITRATE REDUCTASE; OXIDOREDUCTASE; PERCHLORATE REDUCTASE; PYROGALLOL PHLOROGLUCINOL TRANSHYDROXYLASE; RESORCINOL HYDROXYLASE; SULFUR REDUCTASE; TETRATHIONATE REDUCTASE; THIOSULFATE REDUCTASE; UNCLASSIFIED DRUG; ENZYME; LIGAND; QUINONE DERIVATIVE;

ALCALIGENES FAECALIS; AQUIFEX AEOLICUS; ARTICLE; AZOARCUS; BACILLUS SELENATARSENATIS; BACILLUS SUBTILIS; BIOENERGY; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; DECHLOROMONAS AROMATICA; DESULFOVIBRIO DESULFURICANS; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ESCHERICHIA COLI; HALOBACTERIUM; HALOFERAX MEDITERRANEI; HALORHODOSPIRA HALOPHILA; IDEONELLA DECHLORATANS; KLEBSIELLA PNEUMONIAE; METHANOTHERMOBACTER THERMAUTOTROPHICUS; NITROBACTER; NONHUMAN; PELOBACTER; PELOBACTER ACETYLENICUS; PHYLOGENY; PRIORITY JOURNAL; PROKARYOTE; PYROBACULUM AEROPHILUM; REACTION ANALYSIS; RHODOBACTER SPHAEROIDES; RHODOVULUM; SALMONELLA TYPHIMURIUM; SEQUENCE ANALYSIS; SHEWANELLA; SHEWANELLA MASSILIA; SYNECHOCOCCUS; THAUERA SELENATIS; THERMUS THERMOPHILUS; WOLINELLA SUCCINOGENES; BIOENERGETIC; CATALYSIS; ENERGY METABOLISM; IRON-SULFUR; METABOLISM; REVIEW;

PROKARYOTA;

BIOENERGETIC; ELECTRON TRANSFER; IRON-SULFUR; MOLYBDENUM; PROKARYOTE; QUINONE;

CATALYSIS; ENERGY METABOLISM; ENZYMES; LIGANDS;

EID: 84884294235     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.01.011     Document Type: Review

References (469)

1. J. Frausto da Silva, R.Williams, The Biological Chemistry of the Elements: The Inorganic Chemistry of Life, Oxford Univ Press, Oxford, UK, 2001.
2. Y. Zhang, V.N. Gladyshev, Molybdoproteomes and evolution of molybdenum utilization, J. Mol. Biol. 379 (2008) 881-899.
3. A. Suyama, R. Iwakiri, K. Kai, T. Tokunaga,N. Sera,K. Furukawa, Isolation and characterization of Desulfitobacterium sp. strain Y51 capable of efficient dehalogenation of tetrachloroethene and polychloroethanes, Biosci. Biotechnol. Biochem. 65 (2001) 1474-1481. (Pubitemid 33617610)
4. H. Nonaka, G. Keresztes, Y. Shinoda, Y. Ikenaga, M. Abe, K. Naito, K. Inatomi, K. Furukawa, M. Inui, H. Yukawa, Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195, J. Bacteriol. 188 (2006) 2262-2274. (Pubitemid 43376480)
5. A. Cvetkovic, A.L.Menon,M.P. Thorgersen, J.W. Scott, F.L. Poole II, F.E. Jenney Jr.,W.A. Lancaster, J.L. Praissman, S. Shanmukh, B.J.Vaccaro, S.A. Trauger, E. Kalisiak, J.V. Apon, G. Siuzdak, S.M. Yannone, J.A. Tainer, M.W. Adams, Microbial metalloproteomes are largely uncharacterized, Nature 466 (2010) 779-782.
6. M.K. Johnson, D.C. Rees, M.W. Adams, Tungstoenzymes, Chem. Rev. 96 (1996) 2817-2840.
7. A. Kletzin, M.W. Adams, Tungsten in biological systems, FEMS Microbiol. Rev. 18 (1996) 5-63. (Pubitemid 26163588)
8. E.J. Dridge, C.S. Butler, Thermostable properties of the periplasmic selenate reductase from Thauera selenatis, Biochimie 92 (2010) 1268-1273.
9. A.D. Anbar, Oceans. Elements and evolution, Science 322 (2008) 1481-1483.
10. O. Einsle, F.A. Tezcan, S.L. Andrade, B. Schmid,M. Yoshida, J.B. Howard, D.C. Rees, Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor, Science 297 (2002) 1696-1700. (Pubitemid 35000783)
11. J.Wilcoxen, B. Zhang, R. Hille, Reaction of themolybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones, Biochemistry 50 (2011) 1910-1916.
12. R.Hille, Themononuclearmolybdenumenzymes, Chem. Rev. 96 (1996) 2757-2816.
13. G. Schwarz, R.R. Mendel, M.W. Ribbe, Molybdenum cofactors, enzymes and pathways, Nature 460 (2009) 839-847.
14. Y. Zhang, S. Rump, V.N. Gladyshev, Comparative genomics and evolution ofmolybdenum utilization, Coord. Chem. Rev. 255 (2011) 1206-1217.
15. F. Schneider, J. Lowe, R. Huber, H. Schindelin, C. Kisker, J. Knablein, Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution, J. Mol. Biol. 263 (1996) 53-69. (Pubitemid 26361512)
16. R.A. Rothery, G.J. Workun, J.H. Weiner, The prokaryotic complex iron-sulfur molybdoenzyme family, Biochim. Biophys. Acta 1778 (2008) 1897-1929.
17. H. Dobbek, Structural aspects of mononuclear Mo/W enzymes, Coord. Chem. Rev. 255 (2011) 1104-1116.
18. R.H. Holm, E.I. solomon, A. Majumdar, A. Tenderhold, Comparative molecular chemistry of molybdenum and tungsten and its relation to hydroxylase and oxotransferase enzymes, Coord. Chem. Rev. 255 (2011) 22.
19. A.Magalon, J.G. Fedor, A.Walburger, J.H.Weiner, Molybdenum enzymes in bacteria and their maturation, Coord. Chem. Rev. 255 (2011) 19.
20. M.J. Romao, Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview, Dalton Trans. (2009) 4053-4068.
21. B. Schink, Fermentation of acetylene by an obligate anaerobe, Pelobacter acetylenicus sp. nov. Arch. Microbiol. 142 (1985) 295-301.
22. A.Messerschmidt, H. Niessen, D. Abt, O. Einsle, B. Schink, P.M. Kroneck, Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols, Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 11571-11576. (Pubitemid 39095337)
23. F. Baymann, E. Lebrun, M. Brugna, B. Schoepp-Cothenet, M.T. Giudici-Orticoni, W. Nitschke, The redox protein construction kit: pre-last universal common ancestor evolution of energy-conserving enzymes, Philos. Trans. R. Soc. Lond. B Biol. Sci. 358 (2003) 267-274. (Pubitemid 36178235)
24. B. Schoepp-Cothenet, R. van Lis, A. Atteia, F. Baymann, L. Capowiez, A.L. Ducluzeau, S. Duval, F. Ten Brink, M.J. Russell,W. Nitschke, On the universal core of bioenergetics, Biochim. Biophys. Acta 1827 (2013) 79-93.
25. B. Schoepp-Cothenet, R. van Lis, P. Philippot, A. Magalon, M.J. Russell, W. Nitschke, The ineluctable requirement for the trans-iron elements molybdenumand/or tungsten in the origin of life, Sci. Rep. 2 (2012) 263.
26. M.J. Russell, A.J. Hall, The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front, J. Geol. Soc. London 154 (1997) 377-402.
27. B.E. Erickson, G.R. Helz, Molybdenum(VI) speciation in sulfidic waters: stability and lability of thiomolybdates, Geochim. Cosmochim. Acta 64 (2000) 1149-1158. (Pubitemid 30239468)
28. W. Nitschke, M.J. Russell, Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge, J. Mol. Evol. 69 (2009) 481-496.
29. J. Simon, M.G. Klotz, Diversity and evolution of bioenergetic systems involved in microbial nitrogen compound transformations, Biochim. Biophys. Acta 1827 (2013) 114-135.
30. J. Simon, R.J. van Spanning, D.J. Richardson, The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems, Biochim. Biophys. Acta 1777 (2008) 1480-1490.
31. J.A. Dumesic, G.W. Huber, M. Boudart, Handbook of Heterogeneous Catalysis, 2nd ed., 2008, pp. 1-15.
32. G.A. Somorjai, Y. Li, Introduction to Surface Chemistry and Catalysis, 2nd ed., John Wiley &Sons, Hoboken, NJ, 2010.
33. M.R. Smith, U.S. Ozkan, Transient isotopic labeling studies under steady-state conditions in partial oxidation of methane to formaldehyde over MoO3 catalysts, J. Catal. 142 (1993) 226-236.
34. M. Pourbaix, Atlas of Electrochemical Equilibria in Aqueous Solutions, 2nd ed. National Association of Corrosion Engineers (NACE International), Houston, 1974.
35. C.A. Trieber, R.A. Rothery, J.H. Weiner, Engineering a novel iron-sulfur cluster into the catalytic subunit of Escherichia coli dimethyl-sulfoxide reductase, J. Biol. Chem. 271 (1996) 4620-4626. (Pubitemid 26074939)
36. L.E. Bevers, P.L. Hagedoorn, W.R. Hagen, The bioinorganic chemistry of tungsten, Coord. Chem. Rev. 253 (2009) 269-290.
37. M.J. Pushie, G.N. George, Spectroscopic studies of molybdenum and tungsten enzymes, Coord. Chem. Rev. 255 (2011) 1055-1084.
38. S. Metz, W. Thiel, Theoretical studies on the reactivity of molybdenum enzymes, Coord. Chem. Rev. 255 (2011) 1085-1103.
39. H. Schindelin, C. Kisker, J. Hilton, K.V. Rajagopalan, D.C. Rees, Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination, Science 272 (1996) 1615-1621. (Pubitemid 26200018)
40. A.S. McAlpine, A.G. McEwan, A.L. Shaw, S. Bailey, Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-A resolution and the ditionite-reduced enzyme at 2.8-A resolution, J. Biol. Inorg. Chem. 2 (1997) 690-701. (Pubitemid 28030877)
41. M. Czjzek, J.P. Dos Santos, J. Pommier, G. Giordano, V.Mejean, R. Haser, Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanellamassilia at 2.5 A resolution, J.Mol. Biol. 284 (1998) 435-447. (Pubitemid 28542464)
42. H.-K. Li, C. Temple, K.V. Rajagopalan, H. Schindelin, The 1.3 A crystal structure of Rhodobacter sphaeroides dimethyl sulfoxide reductase reveals two distinct molybdenum coordination environments, J. Am. Chem. Soc. 122 (2000) 7673-7680.
43. G.N. George, J. Hilton, K.V. Rajagoapalan, X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides, J. Am. Chem. Soc. 118 (1996) 1113-1117. (Pubitemid 26075548)
44. G.N. George, J. Hilton, C. Temple, R.C. Prince, K.V. Rajagoapalan, Structure of the molybdenum site of dimethyl sulfoxide reductase, J. Am. Chem. Soc. 121 (1999) 1256-1266.
45. S.D. Garton, J. Hilton, H. Oku, B.R. Crouse, K.V. Rajagoapalan,M.K. Johnson, Active site structures and catalytic mechanism of Rhodobacter sphaeroides dimethyl sulfoxide reductase as revealed by resonance Raman spectroscopy, J. Am. Chem. Soc. 119 (1997) 12906-12916. (Pubitemid 28108870)
46. L. Zhang, K.J. Nelson, K.V. Rajagopalan, G.N. George, Structure of themolybdenumsite of Escherichia coli trimethylamine N-oxide reductase, Inorg. Chem. 47 (2008) 1074-1078.
47. V. Fourmond, B. Burlat, S. Dementin, P. Arnoux, M. Sabaty, S. Boiry, B. Guigliarelli, P. Bertrand, D. Pignol, C. Leger, Major Mo(V) EPR signature of Rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family, J. Phys. Chem. B 112 (2008) 15478-15486.
48. R.C. Bray, B. Adams, A.T. Smith, B. Bennett, S. Bailey, Reversible dissociation of thiolate ligands frommolybdenumin an enzyme of the dimethyl sulfoxide reductase family, Biochemistry 39 (2000) 11258-11269.
49. A.S. McAlpine, A.G. McEwan, S. Bailey, The high resolution crystal structure of DMSO reductase in complex with DMSO, J. Mol. Biol. 275 (1998) 613-623. (Pubitemid 28064205)
50. C.E. Webster, M.B. Hall, The theoretical transition state structure of a model complex bears a striking resemblance to the active site structure of DMSO reductase, J. Am. Chem. Soc. 123 (2001) 5820-5821. (Pubitemid 32904725)
51. A. Thapper, R.J. Deeth, E. Nordlander, A density functional study of oxygen atom transfer reactions between biological oxygen atom donors and molybdenum(IV) bis(dithiolene) complexes, Inorg. Chem. 41 (2002) 6695-6702.
52. J.P.McNamara, J.A. Joule, I.H. Hillier, C.D. Garner, Promotion of oxygen atomtransfer in Mo and W enzymes by bicyclic forms of the pterin cofactor, Chem. Commun. (Camb.) (2005) 177-179.
53. N. Cobb, T. Conrads, R. Hille, Mechanistic studies of Rhodobacter sphaeroides Me2SO reductase, J. Biol. Chem. 280 (2005) 11007-11017. (Pubitemid 40418403)
54. N.R. Bastian, C.J. Kay, M.J. Barber, K.V. Rajagopalan, Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans, J. Biol. Chem. 266 (1991) 45-51. (Pubitemid 21906087)
55. B. Bennett, N. Benson, A.G. McEwan, R.C. Bray, Multiple states of the molybdenum centre of dimethylsulphoxide reductase from Rhodobacter capsulatus revealed by EPR spectroscopy, Eur. J. Biochem. 225 (1994) 321-331. (Pubitemid 24306257)
56. A.M. Raitsimring, A.V. Astashkin, C. Feng, J.H. Enemark, K.J. Nelson, K.V. Rajagopalan, Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase, J. Biol. Inorg. Chem. 8 (2003) 95-104. (Pubitemid 36168897)
57. P. Bertrand, B. Guigliarelli, J.P. Gayda, P. Beardwood, J.F. Gibson, A ligand-fieldmodel to describe a new class of 2Fe-2S clusters in proteins and their synthetic analogues, Biochim. Biophys. Acta 831 (1985) 261-266. (Pubitemid 15242685)
58. F. Biaso, B. Burlat, B. Guigliarelli, DFT investigation of the molybdenum cofactor in periplasmic nitrate reductases: structure of the Mo(V) EPR-active species, Inorg. Chem. 51 (2012) 3409-3419.
59. R.P. Mtei, G. Lyashenko, B. Stein, N. Rubie, R. Hille, M.L. Kirk, Spectroscopic and electronic structure studies of a dimethyl sulfoxide reductase catalytic intermediate: implications for electron- and atom-transfer reactivity, J. Am. Chem. Soc. 133 (2011) 9762-9774.
60. J.L. Simala-Grant, J.H. Weiner, Modulation of the substrate specificity of Escherichia coli dimethylsulfoxide reductase, Eur. J. Biochem. 251 (1998) 510-515. (Pubitemid 28080954)
61. J.P. Ridge, K.F. Aguey-Zinsou, P.V. Bernhardt, G.R. Hanson, A.G. McEwan, The critical role of tryptophan-116 in the catalytic cycle of dimethylsulfoxide reductase from Rhodobacter capsulatus, FEBS Lett. 563 (2004) 197-202. (Pubitemid 38471598)
62. N. Cobb, C. Hemann, G.A. Polsinelli, J.P. Ridge, A.G. McEwan, R. Hille, Spectroscopic and kinetic studies of Y114F and W116F mutants of Me2SO reductase from Rhodobacter capsulatus, J. Biol. Chem. 282 (2007) 35519-35529. (Pubitemid 350277113)
63. V.V. Pollock, R.C. Conover, M.K. Johnson, M.J. Barber, Biotin sulfoxide reductase: tryptophan 90 is required for efficient substrate utilization, Arch. Biochem. Biophys. 409 (2003) 315-326. (Pubitemid 36259599)
64. K.E. Johnson, K.V. Rajagopalan, An active site tyrosine influences the ability of the dimethyl sulfoxide reductase family of molybdopterin enzymes to reduce S-oxides, J. Biol. Chem. 276 (2001) 13178-13185.
65. J. Buc, C.L. Santini, R. Giordani, M. Czjzek, L.F. Wu, G. Giordano, Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli, Mol. Microbiol. 32 (1999) 159-168. (Pubitemid 29164143)
66. J.P. Ridge, K.F. Aguey-Zinsou, P.V. Bernhardt, I.M. Brereton, G.R. Hanson, A.G. McEwan, Site-directed mutagenesis of dimethyl sulfoxide reductase from Rhodobacter capsulatus: characterization of a Y114→F mutant, Biochemistry 41 (2002) 15762-15769. (Pubitemid 36062481)
67. J.M. Dias,M.E. Than,A.Humm, R.Huber, G.P. Bourenkov,H.D. Bartunik, S. Bursakov, J. Calvete, J. Caldeira, C. Carneiro, J.J. Moura, I. Moura, M.J. Romao, Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods, Struct. Fold. Des. 7 (1999) 65-79. (Pubitemid 29159183)
68. P. Arnoux, M. Sabaty, J. Alric, B. Frangioni, B. Guigliarelli, J.M. Adriano, D. Pignol, Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase, Nat. Struct. Biol. 10 (2003) 928-934. (Pubitemid 37386102)
69. B.J. Jepson, S. Mohan, T.A. Clarke, A.J. Gates, J.A. Cole, C.S. Butler, J.N. Butt, A.M. Hemmings, D.J. Richardson, Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli, J. Biol. Chem. 282 (2007) 6425-6437. (Pubitemid 47100849)
70. S. Najmudin, P.J. Gonzalez, J. Trincao, C. Coelho, A. Mukhopadhyay, N.M. Cerqueira, C.C. Romao, I. Moura, J.J. Moura, C.D. Brondino, M.J. Romao, Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum, J. Biol. Inorg. Chem. 13 (2008) 737-753.
71. C. Coelho, P.J. Gonzalez, J.G. Moura, I. Moura, J. Trincao, M. Joao Romao, The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states, J. Mol. Biol. 408 (2011) 932-948.
72. M. Leopoldini, N. Russo, M. Toscano, M. Dulak, T.A. Wesolowski, Mechanism of nitrate reduction by Desulfovibrio desulfuricans nitrate reductase-a theoretical investigation, Chemistry 12 (2006) 2532-2541.
73. M. Hoffmann, Density functional theory studies of model complexes for molybdenum-dependent nitrate reductase active sites, J. Biol. Inorg. Chem. 12 (2007) 989-1001.
74. P.J. Gonzalez, M.G. Rivas, C.D. Brondino, S.A. Bursakov, I. Moura, J.J. Moura, EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774, J. Biol. Inorg. Chem. 11 (2006) 609-616. (Pubitemid 43945772)
75. C.S. Butler, J.M. Charnock, B. Bennett, H.J. Sears, A.J. Reilly, S.J. Ferguson, C.D. Garner, D.J. Lowe, A.J. Thomson, B.C. Berks, D.J. Richardson, Models for molybdenum coordination during the catalytic cycle of periplasmic nitrate reductase from Paracoccus denitrificans derived from EPR and EXAFS spectroscopy, Biochemistry 38 (1999) 9000-9012.
76. C.S. Butler, S.A. Fairhurst, S.J. Ferguson, A.J. Thomson, B.C. Berks, D.J. Richardson, D.J. Lowe, Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy, Biochem. J. 363 (2002) 817-823. (Pubitemid 34526404)
77. C. Leger, S.J. Elliott, K.R. Hoke, L.J. Jeuken, A.K. Jones, F.A. Armstrong, Enzyme electrokinetics: using protein film voltammetry to investigate redox enzymes and their mechanisms, Biochemistry 42 (2003) 8653-8662. (Pubitemid 36899807)
78. L.J. Anderson, D.J. Richardson, J.N. Butt, Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemicalmodulation of enzyme activity, Biochemistry 40 (2001) 11294-11307. (Pubitemid 32911272)
79. B. Frangioni, P. Arnoux, M. Sabaty, D. Pignol, P. Bertrand, B. Guigliarelli, C. Leger, In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer, J. Am. Chem. Soc. 126 (2004) 1328-1329. (Pubitemid 38200789)
80. P. Bertrand, B. Frangioni, S. Dementin,M. Sabaty, P. Arnoux, B. Guigliarelli, D. Pignol, C. Leger, Effects of slow substrate binding and release in redox enzymes: theory and application to periplasmic nitrate reductase, J. Phys. Chem. B 111 (2007) 10300-10311. (Pubitemid 47388037)
81. N.M. Cerqueira, P.J. Gonzalez, C.D. Brondino,M.J. Romao, C.C. Romao, I.Moura, J.J. Moura, The effect of the sixth sulfur ligand in the catalytic mechanism of periplasmic nitrate reductase, J. Comput. Chem. 30 (2009) 2466-2484.
82. M. Hofmann, Density functional theory study of model complexes for the revised nitrate reductase active site in Desulfovibrio desulfuricans NapA, J. Biol. Inorg. Chem. 14 (2009) 1023-1035.
83. H. Xie, Z. Cao, Enzymatic reduction of nitrate to nitrite: insight from density functional calculations, Organometallics 29 (2010) 436-441.
84. S. Dementin, P. Arnoux, B. Frangioni, S. Grosse, C. Leger, B. Burlat, B. Guigliarelli, M. Sabaty, D. Pignol, Access to the active site of periplasmic nitrate reductase: insights from site-directed mutagenesis and zinc inhibition studies, Biochemistry 46 (2007) 9713-9721. (Pubitemid 47328577)
85. V. Fourmond, B. Burlat, S.Dementin,M. Sabaty, P. Arnoux, E. Etienne, B.Guigliarelli, P. Bertrand, D. Pignol, C. Leger, Dependence of catalytic activity on driving force in solution assays and protein film voltammetry: insights from the comparison of nitrate reductase mutants, Biochemistry 49 (2010) 2424-2432.
86. T. Hettmann, R.A. Siddiqui, C. Frey, T. Santos-Silva, M.J. Romao, S. Diekmann, Mutagenesis study on amino acids around the molybdenum centre of the periplasmic nitrate reductase from Ralstonia eutropha, Biochem. Biophys. Res. Commun. 320 (2004) 1211-1219. (Pubitemid 38916673)
87. B.J. Jepson, L.J. Anderson, L.M. Rubio, C.J. Taylor, C.S. Butler, E. Flores, A. Herrero, J.N. Butt, D.J. Richardson, Tuning a nitrate reductase for function. The first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties, J. Biol. Chem. 279 (2004) 32212-32218. (Pubitemid 39014669)
88. M. Jormakka, K. Yokoyama, T. Yano, M. Tamakoshi, S. Akimoto, T. Shimamura, P. Curmi, S. Iwata, Molecular mechanism of energy conservation in polysulfide respiration, Nat. Struct. Mol. Biol. 15 (2008) 730-737. (Pubitemid 351931998)
89. T. Prisner, S. Lyubenova, Y. Atabay, F. MacMillan, A. Kroger, O. Klimmek, Multifrequency cw-EPR investigation of the catalytic molybdenum cofactor of polysulfide reductase fromWolinella succinogenes, J. Biol. Inorg. Chem. 8 (2003) 419-426. (Pubitemid 36578193)
90. S. Lyubenova, T. Maly, K. Zwicker, U. Brandt, B. Ludwig, T. Prisner, Multifrequency pulsed electron paramagnetic resonance on metalloproteins, Acc. Chem. Res. 43 (2010) 181-189.
91. J.C. Boyington, V.N. Gladyshev, S.V. Khangulov, T.C. Stadtman, P.D. Sun, Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster, Science 275 (1997) 1305-1308. (Pubitemid 27114158)
92. M. Jormakka, S. Tornroth, B. Byrne, S. Iwata, Molecular basis of proton motive force generation: structure of formate dehydrogenase-N, Science 295 (2002) 1863-1868. (Pubitemid 34214117)
93. H. Raaijmakers, S. Macieira, J.M. Dias, S. Teixeira, S. Bursakov, R. Huber, J.J. Moura, I. Moura, M.J. Romao, Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas, Structure 10 (2002) 1261-1272. (Pubitemid 35254014)
94. H.C. Raaijmakers, M.J. Romao, Formate-reduced E. coli formate dehydrogenase H: the reinterpretation of the crystal structure suggests a new reaction mechanism, J. Biol. Inorg. Chem. 11 (2006) 849-854. (Pubitemid 44337586)
95. G.N. George, C.M. Colangelo, J. Dong, R.A. Scott, S.V. Khangulov, V.N. Gladyshev, T.C. Stadtman, X-ray absorption spectroscopy of the molybdenum site of Escherichia coli formate dehydrogenase, J. Am. Chem. Soc. 120 (1998) 1267-1273. (Pubitemid 28179043)
96. R. Thome, A. Gust, R. Toci, R. Mendel, F. Bittner, A. Magalon, A. Walburger, A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli, J. Biol. Chem. 287 (2012) 4671-4678.
97. S.V. Khangulov, V.N. Gladyshev, G.C. Dismukes, T.C. Stadtman, Seleniumcontaining formate dehydrogenaseHfromEscherichia coli: amolybdopterinenzyme that catalyzes formate oxidation without oxygen transfer, Biochemistry 37 (1998) 3518-3528. (Pubitemid 28125580)
98. M.G. Rivas, P.J.Gonzalez, C.D. Brondino, J.J.Moura, I.Moura, EPR characterization of the molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774 upon formate reduction, J. Inorg. Biochem. 101 (2007) 1617-1622. (Pubitemid 47576187)
99. L. De Gioia, P. Fantucci, B. Guigliarelli, P. Bertrand, Ab initio investigation of the structural and electronic differences between active-site models of NiFe and NiFe Se hydrogenases, Int. J. Quantum Chem. 73 (1999) 187-195. (Pubitemid 129648482)
100. M.J.Axley,A. Bock, T.C. Stadtman, Catalytic properties of an Escherichia coli formate dehydrogenasemutant inwhich sulfur replaces selenium, Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 8450-8454. (Pubitemid 21915374)
101. M. Leopoldini, S.G. Chiodo, M. Toscano, N. Russo, Reaction mechanism of molybdoenzyme formate dehydrogenase, Chemistry 14 (2008) 8674-8681.
102. C.S. Mota, M.G. Rivas, C.D. Brondino, I. Moura, J.J. Moura, P.J. Gonzalez, N.M. Cerqueira, The mechanism of formate oxidation by metal-dependent formate dehydrogenases, J. Biol. Inorg. Chem. 16 (2011) 1255-1268.
103. M. Tiberti, E. Papaleo, N. Russo, L. De Gioia, G. Zampella, Evidence for the formation of a Mo-H intermediate in the catalytic cycle of formate dehydrogenase, Inorg. Chem. 51 (2012) 8331-8339.
104. G.B. Seiffert, G.M. Ullmann, A. Messerschmidt, B. Schink, P.M. Kroneck, O. Einsle, Structure of the non-redox-active tungsten/4Fe4S enzyme acetylene hydratase, Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 3073-3077 (Pubitemid 46364115)
105. F. Tenbrink, B. Schink, P.M. Kroneck, Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase, J. Bacteriol. 193 (2011) 1229-1236.
106. S. Antony, C.A. Bayse, Theoretical studies of models of the active site of the tungstoenzyme acetylene hydratase, Organometallics 28 (2009) 4938-4944.
107. M.A. Vincent, I.H. Hillier, G. Periyasamy, N.A. Burton, A DFT study of the possible role of vinylidene and carbene intermediates in the mechanism of the enzyme acetylene hydratase, Dalton Trans. 39 (2010) 3816-3822.
108. R.Z. Liao, J.G. Yu, F. Himo, Mechanism of tungsten-dependent acetylene hydratase from quantum chemical calculations, Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 22523-22527.
109. Y.F. Liu, R.Z. Liao, W.J. Ding, J.G. Yu, R.Z. Liu, Theoretical investigation of the first-shell mechanism of acetylene hydration catalyzed by a biomimetic tungsten complex, J. Biol. Inorg. Chem. 16 (2011) 745-752.
110. R.C. Bray, S.P. Vincent, D.J. Lowe, R.A. Clegg, P.B. Garland, Electron-paramagneticresonance studies on the molybdenum of nitrate reductase from Escherichia coli K12, Biochem. J. 155 (1976) 201-203.
111. B. Guigliarelli, M. Asso, C. More, V. Augier, F. Blasco, J. Pommier, G. Giordano, P. Bertrand, EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z fromEscherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism, Eur. J. Biochem. 207 (1992) 61-68.
112. B. Guigliarelli, A. Magalon, M. Asso, P. Bertrand, C. Frixon, G. Giordano, F. Blasco, Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of sitedirected mutants lacking the highest or lowest potential 4Fe-4S clusters, Biochemistry 35 (1996) 4828-4836.
113. F. Blasco, B. Guigliarelli, A.Magalon,M. Asso, G. Giordano, R.A. Rothery, The coordination and function of the redox centres of the membrane-bound nitrate reductases, Cell. Mol. Life Sci. 58 (2001) 179-193. (Pubitemid 32217350)
114. M.G. Bertero, R.A. Rothery, M. Palak, C. Hou, D. Lim, F. Blasco, J.H. Weiner, N.C. Strynadka, Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A, Nat. Struct. Biol. 10 (2003) 681-687. (Pubitemid 37052404)
115. M. Jormakka, D. Richardson, B. Byrne, S. Iwata, Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes, Structure (Camb) 12 (2004) 95-104. (Pubitemid 38114809)
116. C. Avazeri, R.J. Turner, J. Pommier, J.H. Weiner, G. Giordano, A. Vermeglio, Tellurite reductase activity of nitrate reductase is responsible for the basal resistance of Escherichia coli to tellurite, Microbiology 143 (Pt 4) (1997) 1181-1189. (Pubitemid 27207787)
117. M. Sabaty, C. Avazeri, D. Pignol, A. Vermeglio, Characterization of the reduction of selenate and tellurite by nitrate reductases, Appl. Environ. Microbiol. 67 (2001) 5122-5126. (Pubitemid 33701279)
118. S.J.Nieter Burgmayer,D.L. Pearsall, S.M. Blaney, E.M.Moore, C. Sauk-Schubert, Redox reactions of the pyranopterin system of the molybdenum cofactor, J. Biol. Inorg. Chem. 9 (2004) 59-66. (Pubitemid 38173668)
119. S.P. Vincent, R.C. Bray, Electron-paramagnetic-resonance studies on nitrate reductase from Escherichia coli K12, Biochem. J. 171 (1978) 639-647. (Pubitemid 8348737)
120. G.N. George, R.C. Bray, F.F. Morpeth, D.H. Boxer, Complexes with halide and other anions of the molybdenum centre of nitrate reductase from Escherichia coli, Biochem. J. 227 (1985) 925-931. (Pubitemid 15044669)
121. G.N. George, N.A. Turner, R.C. Bray, F.F. Morpeth, D.H. Boxer, S.P. Cramer, X-ray-absorption and electron-paramagnetic-resonance spectroscopic studies of the environment of molybdenum in high-pH and low-pH forms of Escherichia coli nitrate reductase, Biochem. J. 259 (1989) 693-700. (Pubitemid 19118834)
122. A. Magalon, M. Asso, B. Guigliarelli, R.A. Rothery, P. Bertrand, G. Giordano, F. Blasco, Molybdenum cofactor properties and Fe-S cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit, Biochemistry 37 (1998) 7363-7370. (Pubitemid 28235219)
123. R.A. Rothery, M.G. Bertero, T. Spreter, N. Bouromand, N.C. Strynadka, J.H. Weiner, Protein crystallography reveals a Role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation, J. Biol. Chem. 285 (2010) 8801-8807.
124. N. Turner, A.L. Ballard, R.C. Bray, S. Ferguson, Investigation by electron paramagnetic resonance spectroscopy of the molybdenum centre of respiratory nitrate reductase from Paracoccus denitrificans, Biochem. J. 252 (1988) 925-926.
125. C. Correia, S. Besson, C.D. Brondino, P.J. Gonzalez, G. Fauque, J. Lampreia, I.Moura, J.J. Moura, Biochemical and spectroscopic characterization of the membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617, J. Biol. Inorg. Chem. 13 (2008) 1321-1333.
126. S.J. Field, N.P. Thornton, L.J. Anderson, A.J. Gates, A. Reilly, B.J. Jepson, D.J. Richardson, S.J. George, M.R. Cheesman, J.N. Butt, Reductive activation of nitrate reductases, Dalton Trans (2005) 3580-3586. (Pubitemid 41609911)
127. J. Marangon, P.M. Paes de Sousa, I. Moura, C.D. Brondino, J.J. Moura, P.J. Gonzalez, Substrate-dependent modulation of the enzymatic catalytic activity: reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617, Biochim. Biophys. Acta 1817 (2012) 1072-1082.
128. C.E. Vine, S.K. Purewal, J.A. Cole, NsrR-dependent method for detecting nitric oxide accumulation in the Escherichia coli cytoplasm and enzymes involved in NO production, FEMS Microbiol. Lett. 325 (2011) 108-114.
129. N.J. Gilberthorpe, R.K. Poole, Nitric oxide homeostasis in Salmonella typhimurium: roles of respiratory nitrate reductase and flavohemoglobin, J. Biol. Chem. 283 (2008) 11146-11154.
130. G. Rowley, D. Hensen, H. Felgate, A. Arkenberg, C. Appia-Ayme, K. Prior, C. Harrington, S.J. Field, J.N. Butt, E. Baggs, D.J. Richardson, Resolving the contributions of the membrane-bound and periplasmic nitrate reductase systems to nitric oxide and nitrous oxide production in Salmonella enterica serovar Typhimurium, Biochem. J. 441 (2012) 755-762.
131. D.P. Kloer, C. Hagel, J. Heider, G.E. Schulz, Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum, Structure 14 (2006) 1377-1388. (Pubitemid 44331613)
132. D. Knack, C. Hagel, M. Szaleniec, A. Dudzik, A. Salwinski, J. Heider, Substrate and inhibitor spectra of ethylbenzene dehydrogenase: perspectives on application potential and catalytic mechanism, Appl. Environ. Microbiol. 78 (2012) 6475-6482.
133. M. Szaleniec, T. Borowski, K. Schuhle, M.Witko, J. Heider, Ab initio modeling of ethylbenzene dehydrogenase reaction mechanism, J. Am. Chem. Soc. 132 (2010) 6014-6024.
134. J. Caldeira, V. Belle, M. Asso, B. Guigliarelli, I. Moura, J.J.G. Moura, P. Bertrand, Analysis of the electron paramagnetic resonance properties of the 2Fe-2S1+ centers in molybdenum enzymes of the xanthine oxidase family: assignment of signals I and II, Biochemistry 39 (2000) 2700-2707. (Pubitemid 30148924)
135. P. Bertrand, C. More, B. Guigliarelli, A. Fournel, B. Bennett, B. Howes, Biological polynuclear clusters coupled by magnetic interactions: from the point dipole approximation to a local spin model, J. Am. Chem. Soc. 116 (1994) 3078-3086. (Pubitemid 24173165)
136. A.V. Astashkin, A. Rajapakshe, M.J. Cornelison, K. Johnson-Winters, J.H. Enemark, Determination of the distance between the Mo(V) and Fe(III) heme centers of wild type human sulfite oxidase by pulsed EPR spectroscopy, J. Phys. Chem. B 116 (2012) 1942-1950.
137. S. Stoll, Y. NejatyJahromy, J.J. Woodward, A. Ozarowski, M.A. Marletta, R.D. Britt, Nitric oxide synthase stabilizes the tetrahydrobiopterin cofactor radical by controlling its protonation state, J. Am. Chem. Soc. 132 (2012) 11812-11823.
138. A. Brunel, J. Santolini, P. Dorlet, Electron paramagnetic resonance characterization of tetrahydrobiopterin radical formation in bacterial nitric oxide synthase compared to mammalian nitric oxide synthase, Biophys. J. 103 (2012) 109-117.
139. R.A. Rothery, B. Stein,M. Solomonson,M.L. Kirk, J.H.Weiner, Pyranopterin conformation defines the function of molybdenum and tungsten enzymes, Proc. Natl. Acad. Sci. U. S. A. 109 (2012) 14773-14778.
140. M.C. Lett, D. Muller, D. Lievremont, S. Silver, J. Santini, Unified nomenclature for genes involved in prokaryotic aerobic arsenite oxidation, J. Bacteriol. 194 (2012) 207-208.
141. D. Muller, D. Lievremont, D.D. Simeonova, J.C. Hubert, M.C. Lett, Arsenite oxidase aox genes from a metal-resistant beta-proteobacterium, J. Bacteriol. 185 (2003) 135-141. (Pubitemid 36008830)
142. V. Bonnefoy, J. Ratouchniak, F. Blasco, M. Chippaux, Organization of the nar genes at the chlZ locus, FEMS Microbiol. Lett. 147 (1997) 147-149. (Pubitemid 27092101)
143. V.M. Luque-Almagro, A.J. Gates, C. Moreno-Vivian, S.J. Ferguson, D.J. Richardson, M.D. Roldan, Bacterial nitrate assimilation: gene distribution and regulation, Biochem. Soc. Trans. 39 (2011) 1838-1843.
144. F.F. Morpeth, D.H. Boxer, Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12, Biochemistry 24 (1985) 40-46.
145. S. Gon, J.C. Patte, V. Mejean, C. Iobbi-Nivol, The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli, J. Bacteriol. 182 (2000) 5779-5786.
146. V.V. Pollock, M.J. Barber, Biotin sulfoxide reductase. Heterologous expression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme, J. Biol. Chem. 272 (1997) 3355-3362.
147. S. Duval, A.L. Ducluzeau, W. Nitschke, B. Schoepp-Cothenet, Enzyme phylogenies as markers for the oxidation state of the environment: the case of respiratory arsenate reductase and related enzymes, BMC Evol. Biol. 8 (2008) 206.
148. M. Hensel, A.P. Hinsley, T. Nikolaus, G. Sawers, B.C. Berks, The genetic basis of tetrathionate respiration in Salmonella typhimurium, Mol. Microbiol. 32 (1999) 275-287. (Pubitemid 29178695)
149. M. Guiral, P. Tron, C. Aubert, A. Gloter, C. Iobbi-Nivol, M.T. Giudici-Orticoni, A membrane-bound multienzyme, hydrogen-oxidizing, and sulfur-reducing complex from the hyperthermophilic bacterium Aquifex aeolicus, J. Biol. Chem. 280 (2005) 42004-42015. (Pubitemid 43023169)
150. N.K. Heinzinger, S.Y. Fujimoto, M.A. Clark, M.S. Moreno, E.L. Barrett, Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism, J. Bacteriol. 177 (1995) 2813-2820.
151. B.J. Jepson, A. Marietou, S. Mohan, J.A. Cole, C.S. Butler, D.J. Richardson, Evolution of the soluble nitrate reductase: defining themonomeric periplasmic nitrate reductase subgroup, Biochem. Soc. Trans. 34 (2006) 122-126. (Pubitemid 43235550)
152. K. Ogawa, E. Akagawa, K. Yamane, Z.W. Sun, M. LaCelle, P. Zuber, M.M. Nakano, The nasB operon and nasA gene are required for nitrate/nitrite assimilation in Bacillus subtilis, J. Bacteriol. 177 (1995) 1409-1413.
153. J.T. Lin, B.S. Goldman, V. Stewart, Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al, J. Bacteriol. 175 (1993) 2370-2378. (Pubitemid 23123513)
154. A.J. Gates, V.M. Luque-Almagro, A.D. Goddard, S.J. Ferguson, M.D. Roldan, D.J. Richardson, A composite biochemical systemfor bacterial nitrate and nitrite assimilation as exemplified by Paracoccus denitrificans, Biochem. J. 435 (2011) 743-753.
155. P. Lanciano, A. Savoyant, S. Grimaldi, A. Magalon, B. Guigliarelli, P. Bertrand, New method for the spin quantitation of 4Fe-4S+ clusters with S=(3)/(2). Application to the FS0 center of the NarGHI nitrate reductase from Escherichia coli, J. Phys. Chem. B 111 (2007) 13632-13637. (Pubitemid 350275468)
156. R.A.Rothery,M.G. Bertero, R. Cammack,M. Palak, F. Blasco,N.C. Strynadka, J.H.Weiner, The catalytic subunit of Escherichia coli nitrate reductase A contains a novel 4Fe-4S cluster with a high-spin ground state, Biochemistry 43 (2004) 5324-5333. (Pubitemid 38620924)
157. T. Krafft, A. Bowen, F. Theis, J.M. Macy, Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis, DNA Seq. 10 (2000) 365-377. (Pubitemid 30308253)
158. C.A. McDevitt, P. Hugenholtz, G.R. Hanson, A.G. McEwan, Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes, Mol. Microbiol. 44 (2002) 1575-1587. (Pubitemid 34639434)
159. H.D. Thorell, K. Stenklo, J. Karlsson, T. Nilsson, A gene cluster for chloratemetabolism in Ideonella dechloratans, Appl. Environ. Microbiol. 69 (2003) 5585-5592. (Pubitemid 37150784)
160. N.L. Creevey, A.G. McEwan, G.R. Hanson, P.V. Bernhardt, Thermodynamic characterization of the redox centers within dimethylsulfide dehydrogenase, Biochemistry 47 (2008) 3770-3776. (Pubitemid 351431367)
161. E.J. Dridge, C.A.Watts, B.J. Jepson, K. Line, J.M. Santini, D.J. Richardson, C.S. Butler, Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy, Biochem. J. 408 (2007) 19-28. (Pubitemid 350158399)
162. C.A. McDevitt, G.R. Hanson, C.J. Noble, M.R. Cheesman, A.G. McEwan, Characterization of the redox centers in dimethyl sulfide dehydrogenase from Rhodovulum sulfidophilum, Biochemistry 41 (2002) 15234-15244. (Pubitemid 36008132)
163. H. Tang, R.A. Rothery, J.E. Voss, J.H. Weiner, Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion, J. Biol. Chem. 286 (2011) 15147-15154.
164. J.A. Muller, S. DasSarma, Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors, J. Bacteriol. 187 (2005) 1659-1667. (Pubitemid 40289366)
165. S. Lucker, M. Wagner, F. Maixner, E. Pelletier, H. Koch, B. Vacherie, T. Rattei, J.S. Damste, E. Spieck, D. Le Paslier, H. Daims, A Nitrospira metagenome illuminates the physiology and evolution of globally important nitrite-oxidizing bacteria, Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 13479-13484.
166. R.M.Martinez-Espinosa, E.J. Dridge,M.J. Bonete, J.N. Butt, C.S. Butler, F. Sargent, D.J. Richardson, Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases, FEMS Microbiol. Lett. 276 (2007) 129-139. (Pubitemid 47621780)
167. J. Dermer, G. Fuchs, Molybdoenzyme that catalyzes the anaerobic hydroxylation of a tertiary carbon atom in the side chain of cholesterol, J. Biol. Chem. 287 (2012) 36905-36916.
168. D.Y. Sorokin, S. Lucker, D. Vejmelkova, N.A. Kostrikina, R. Kleerebezem,W.I. Rijpstra, J.S. Damste, D. Le Paslier, G. Muyzer, M. Wagner, M.C. van Loosdrecht, H. Daims, Nitrification expanded: discovery, physiology and genomics of a nitrite-oxidizing bacterium from the phylum Chloroflexi, ISME J. 6 (2012) 2245-2256.
169. P.J. Ellis, T. Conrads, R. Hille, P. Kuhn, Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A, Structure 9 (2001) 125-132. (Pubitemid 32209187)
170. S.J. Coulthurst, A. Dawson, W.N. Hunter, F. Sargent, Conserved signal peptide recognition systems across the prokaryotic domains, Biochemistry 51 (2012) 1678-1686.
171. A.P. Hinsley, N.R. Stanley, T. Palmer, B.C. Berks, A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif, FEBS Lett. 497 (2001) 45-49. (Pubitemid 32480178)
172. F. Reyes,M.D. Roldan,W. Klipp, F. Castillo, C.Moreno-Vivian, Isolation of periplasmic nitrate reductase genes fromRhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases, Mol. Microbiol. 19 (1996) 1307-1318. (Pubitemid 26111502)
173. B. Ize, S.J. Coulthurst, K. Hatzixanthis, I. Caldelari, G. Buchanan, E.C. Barclay, D.J. Richardson, T. Palmer, F. Sargent, Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains, Microbiology 155 (2009) 3992-4004.
174. R.J. Turner, A.L. Papish, F. Sargent, Sequence analysis of bacterial redox enzyme maturation proteins (REMPs), Can. J. Microbiol. 50 (2004) 225-238. (Pubitemid 38903410)
175. A. Lieutaud, R. van Lis, S. Duval, L. Capowiez, D. Muller, R. Lebrun, S. Lignon, M.L. Fardeau, M.C. Lett, W. Nitschke, B. Schoepp-Cothenet, Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes, J. Biol. Chem. 285 (2010) 20433-20441.
176. J.M. Santini, R.N. vanden Hoven, Molybdenum-containing arsenite oxidase of the chemolithoautotrophic arsenite oxidizer NT-26, J. Bacteriol. 186 (2004) 1614-1619. (Pubitemid 38314506)
177. M. Kuroda,M. Yamashita, E.Miwa, K. Imao, N. Fujimoto, H. Ono, K. Nagano, K. Sei,M. Ike, Molecular cloning and characterization of the srdBCA operon, encoding the respiratory selenate reductase complex, from the selenate-reducing bacteriumBacillus selenatarsenatis SF-1, J. Bacteriol. 193 (2011) 2141-2148.
178. C.W. Saltikov, D.K. Newman, Genetic identification of a respiratory arsenate reductase, Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10983-10988. (Pubitemid 37140139)
179. J.T. Lin, B.S. Goldman, V. Stewart, The nasFEDCBA operon for nitrate and nitrite assimilation in Klebsiella pneumoniae M5al, J. Bacteriol. 176 (1994) 2551-2559. (Pubitemid 24139033)
180. E. Lebrun, J.M. Santini,M. Brugna, A.L.Ducluzeau, S.Ouchane, B. Schoepp-Cothenet, F. Baymann, W. Nitschke, The Rieske protein: a case study on the pitfalls of multiple sequence alignments and phylogenetic reconstruction, Mol. Biol. Evol. 23 (2006) 1180-1191. (Pubitemid 43781593)
181. S. Duval, J.M. Santini, W. Nitschke, R. Hille, B. Schoepp-Cothenet, The small subunit AroB of arsenite oxidase: lessons on the 2Fe-2S Rieske protein superfamily, J. Biol. Chem. 285 (2010) 20442-20451.
182. R. van Lis, W. Nitschke, S. Duval, B. Schoepp-Cothenet, Arsenics as bioenergetic substrates, Biochim. Biophys. Acta 1827 (2013) 176-188.
183. R. van Lis,W. Nitschke, T.P.Warelow, L. Capowiez, J.M. Santini, B. Schoepp-Cothenet, Heterologously expressed arsenite oxidase: a system to study biogenesis and structure/function relationships of the enzyme family, Biochim. Biophys. Acta 1817 (2012) 1701-1708.
184. R. Blasco, F. Castillo, M. Martinez-Luque, The assimilatory nitrate reductase from the phototrophic bacterium, Rhodobacter capsulatus E1F1, is a flavoprotein, FEBS Lett. 414 (1997) 45-49. (Pubitemid 27380352)
185. C. Costa, M. Teixeira, J. LeGall, J.J.G. Moura, I. Moura, Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774: isolation and spectroscopic characterization of the active sites (heme, iron-sulfur centers andmolybdenum), J. Biol. Inorg. Chem. 2 (1997) 198-208. (Pubitemid 27187579)
186. C. Sebban, L. Blanchard, M. Bruschi, F. Guerlesquin, Purification and characterization of the formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, FEMS Microbiol. Lett. 133 (1995) 143-149.
187. K.S. Bender, C. Shang, R. Chakraborty, S.M. Belchik, J.D. Coates, L.A. Achenbach, Identification, characterization, and classification of genes encoding perchlorate reductase, J. Bacteriol. 187 (2005) 5090-5096. (Pubitemid 41022926)
188. F. Cava, O. Zafra, J. Berenguer, A cytochrome c containing nitrate reductase plays a role in electron transport for denitrification in Thermus thermophilus without involvement of the bc respiratory complex, Mol. Microbiol. 70 (2008) 507-518.
189. O. Zafra, F. Cava, F. Blasco, A. Magalon, J. Berenguer, Membrane-associated maturation of the heterotetrameric nitrate reductase of Thermus thermophilus, J. Bacteriol. 187 (2005) 3990-3996. (Pubitemid 40827782)
190. O. Zafra, S. Ramirez, P. Castan, R. Moreno, F. Cava, C. Valles, E. Caro, J. Berenguer, A cytochrome c encoded by the nar operon is required for the synthesis of active respiratory nitrate reductase in Thermus thermophilus, FEBS Lett. 523 (2002) 99-102. (Pubitemid 34786066)
191. S. Afshar, E. Johnson, S. de Vries, I. Schroder, Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum, J. Bacteriol. 183 (2001) 5491-5495. (Pubitemid 32880576)
192. S. de Vries, M. Momcilovic, M.J. Strampraad, J.P. Whitelegge, A. Baghai, I. Schroder, Adaptation to a high-tungsten environment: Pyrobaculum aerophilum contains an active tungsten nitrate reductase, Biochemistry 49 (2010) 9911-9921.
193. I. Schroder, S. Rech, T. Krafft, J.M.Macy, Purification and characterization of the selenate reductase from Thauera selenatis, J. Biol. Chem. 272 (1997) 23765-23768. (Pubitemid 27410953)
194. T. Nilsson, M. Rova, A. Smedja Backlund, Microbial metabolism of oxochlorates: a bioenergetic perspective, Biochim. Biophys. Acta 1827 (2013) 189-197.
195. H. Hussain, J. Grove, L. Griffiths, S. Busby, J. Cole, A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria, Mol. Microbiol. 12 (1994) 153-163. (Pubitemid 24197453)
196. W. Dietrich, O. Klimmek, The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes, Eur. J. Biochem. 269 (2002) 1086-1095. (Pubitemid 34175367)
197. J.H. Weiner, G. Shaw, R.J. Turner, C.A. Trieber, The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli, J. Biol. Chem. 268 (1993) 3238-3244. (Pubitemid 23070951)
198. L. Pieulle, X. Morelli, P. Gallice, E. Lojou, P. Barbier, M. Czjzek, P. Bianco, F. Guerlesquin, E.C. Hatchikian, The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway, J. Mol. Biol. 354 (2005) 73-90. (Pubitemid 41527215)
199. R.O. Louro, Proton thrusters: overview of the structural and functional features of soluble tetrahaem cytochromes c3, J. Biol. Inorg. Chem. 12 (2007) 1-10. (Pubitemid 44885505)
200. T.M. Iverson, D.M. Arciero, A.B. Hooper, D.C. Rees, High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea, J. Biol. Inorg. Chem. 6 (2001) 390-397. (Pubitemid 32822129)
201. S.R. Starkenburg, P.S. Chain, L.A. Sayavedra-Soto, L. Hauser, M.L. Land, F.W. Larimer, S.A. Malfatti, M.G. Klotz, P.J. Bottomley, D.J. Arp, W.J. Hickey, Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255, Appl. Environ. Microbiol. 72 (2006) 2050-2063.
202. S.R. Starkenburg, F.W. Larimer, L.Y. Stein, M.G. Klotz, P.S. Chain, L.A. Sayavedra-Soto, A.T. Poret-Peterson,M.E. Gentry, D.J. Arp, B.Ward, P.J. Bottomley, Complete genome sequence of Nitrobacter hamburgensis X14 and comparative genomic analysis of species within the genus Nitrobacter, Appl. Environ.Microbiol. 74 (2008) 2852-2863. (Pubitemid 351632616)
203. P.N. Refojo, M. Teixeira, M.M. Pereira, The alternative complex III: properties and possible mechanisms for electron transfer and energy conservation, Biochim. Biophys. Acta 1817 (2012) 1852-1859.
204. M.L. Rodrigues, T.F. Oliveira, I.A. Pereira, M. Archer, X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination, EMBO J. 25 (2006) 5951-5960. (Pubitemid 44967776)
205. V. Mejean, C. Iobbi-Nivol, M. Lepelletier, G. Giordano, M. Chippaux, M.C. Pascal, TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon, Mol. Microbiol. 11 (1994) 1169-1179. (Pubitemid 24201632)
206. T. Ujiiye, I. Yamamoto, H. Nakama, A. Okubo, S. Yamazaki, T. Satoh, Nucleotide sequence of the genes, encoding the pentaheme cytochrome (dmsC) and the transmembrane protein (dmsB), involved in dimethyl sulfoxide respiration from Rhodobacter sphaeroides f. sp. denitrificans, Biochim. Biophys. Acta 1277 (1996) 1-5. (Pubitemid 26388871)
207. M.D. Roldan, H.J. Sears, M.R. Cheesman, S.J. Ferguson, A.J. Thomson, B.C. Berks, D.J. Richardson, Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport, J. Biol. Chem. 273 (1998) 28785-28790. (Pubitemid 28507568)
208. J.N. Murphy, C.W. Saltikov, The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species, J. Bacteriol. 189 (2007) 2283-2290. (Pubitemid 46411342)
209. S. Gon, M.T. Giudici-Orticoni, V. Mejean, C. Iobbi-Nivol, Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli, J. Biol. Chem. 276 (2001) 11545-11551.
210. A.L. Shaw, A. Hochkoeppler, P. Bonora, D. Zannoni, G.R. Hanson, A.G. McEwan, Characterization of DorC from Rhodobacter capsulatus, a c-type cytochrome involved in electron transfer to dimethyl sulfoxide reductase, J. Biol. Chem. 274 (1999) 9911-9914.
211. T.H. Brondijk, A. Nilavongse, N. Filenko, D.J. Richardson, J.A. Cole, 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 (2004) 47-55. (Pubitemid 38491358)
212. M. Kern, J. Simon, Characterization of the NapGH quinol dehydrogenase complex involved in Wolinella succinogenes nitrate respiration, Mol. Microbiol. 69 (2008) 1137-1152.
213. B. Schoepp-Cothenet, C. Lieutaud, F. Baymann, A. Vermeglio, T. Friedrich, D.M. Kramer, W. Nitschke, Menaquinone as pool quinone in a purple bacterium, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 8549-8554.
214. W. Nitschke, D.M. Kramer, A. Riedel, U. Liebl, From naphto- to benzoquinones, (r)evolutionary reorganisation of electron transfer chains, in: P.Mathis (Ed.), Photosynthesis: From Light to Biosphere, Kluwer Academic Publishers, Dortrecht, 1995, pp. 945-950.
215. M.D. Collins, D. Jones, Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication, Microbiol. Rev. 45 (1981) 316-354. (Pubitemid 11032202)
216. S. Grimaldi, P. Lanciano, P. Bertrand, F. Blasco, B. Guigliarelli, Evidence for an EPR-detectable semiquinone intermediate stabilized in the membrane-bound subunit NarI of nitrate reductase A (NarGHI) from Escherichia coli, Biochemistry 44 (2005) 1300-1308. (Pubitemid 40209009)
217. S. Grimaldi, R. Arias-Cartin, P. Lanciano, S. Lyubenova, R. Szenes, B. Endeward, T.F. Prisner, B. Guigliarelli, A. Magalon, Determination of the proton environment of high stability Menasemiquinone intermediate in Escherichia coli nitrate reductase A by pulsed EPR, J. Biol. Chem. 287 (2012) 4662-4670.
218. R. Arias-Cartin, S. Grimaldi, J. Pommier, P. Lanciano, C. Schaefer, P. Arnoux, G. Giordano, B. Guigliarelli, A. Magalon, Cardiolipin-based respiratory complex activation in bacteria, Proc. Natl. Acad. Sci. U. S. A. 108 (2011) 7781-7786.
219. P. Lanciano, A. Magalon, P. Bertrand, B. Guigliarelli, S. Grimaldi, High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD, Biochemistry 46 (2007) 5323-5329. (Pubitemid 46717256)
220. S. Grimaldi, R. Arias-Cartin, P. Lanciano, S. Lyubenova, B. Endeward, T.F. Prisner, A. Magalon, B. Guigliarelli, Direct evidence for nitrogen ligation to the high stability semiquinone intermediate in Escherichia coli nitrate reductase A, J. Biol. Chem. 285 (2010) 179-187.
221. R. Arias-Cartin, S. Lyubenova, P. Ceccaldi, T. Prisner, A. Magalon, B. Guigliarelli, S. Grimaldi, HYSCORE evidence that endogenous mena- and ubisemiquinone bind at the same Q site (Q(D)) of Escherichia coli nitrate reductase A, J. Am. Chem. Soc. 132 (2010) 5942-5943.
222. U. Liebl, S. Pezennec, A. Riedel, E. Kellner, W. Nitschke, The Rieske FeS center from the gram-positive bacterium PS3 and its interaction with the menaquinone pool studied by EPR, J. Biol. Chem. 267 (1992) 14068-14072.
223. G.M. Carlone, F.A. Anet, Detection ofmenaquinone-6 and a novelmethyl-substituted menaquinone-6 in Campylobacter jejuni and Campylobacter fetus subsp. fetus, J. Gen. Microbiol. 129 (1983) 3385-3393. (Pubitemid 14200355)
224. M.D. Collins, F. Fernandez, Menaquinone-6 and thermoplasma-quinone-6 in Wolinella succinogenes, FEMS Microbiol. Lett. 22 (1984) 273-276.
225. T. Itoh, H. Funabashi, Y. Katayama-Fujimura, S. Iwasaki, H. Kuraishi, Structure of methylmenaquinone-7 isolated from Alteromonas putrefaciens, Biochim. Biophys. Acta 840 (1985) 51-55. (Pubitemid 15042014)
226. M. Akagawa-Matsushita, T. Itoh, Y. Katayama, H. Kuraishi, K. Yamasato, Isoprenoid quinone composition of some marine Alteromonas, Marinomonas, Deleya, Pseudomonas and Shewanella species, J. Gen. Microbiol. 138 (1992) 2275-2281.
227. R. Thummer, O. Klimmek, R.A. Schmitz, Biochemical studies of Klebsiella pneumoniae NifL reduction using reconstituted partial anaerobic respiratory chains of Wolinella succinogenes, J. Biol. Chem. 282 (2007) 12517-12526. (Pubitemid 47100626)
228. B. Nowicka, J. Kruk, Occurrence, biosynthesis and function of isoprenoid quinones, Biochim. Biophys. Acta 1797 (2010) 1587-1605.
229. A.I. Shestopalov, A.V. Bogachev, R.A. Murtazina, M.B. Viryasov, V.P. Skulachev, Aeration-dependent changes in composition of the quinone pool in Escherichia coli. Evidence of post-transcriptional regulation of the quinone biosynthesis, FEBS Lett. 404 (1997) 272-274. (Pubitemid 27113466)
230. B.J. Wallace, I.G. Young, 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 (1977) 84-100. (Pubitemid 8120603)
231. M. Bekker, G. Kramer, A.F. Hartog, M.J. Wagner, C.G. de Koster, K.J. Hellingwerf, M.J. de Mattos, Changes in the redox state and composition of the quinone pool of Escherichia coli during aerobic batch-culture growth, Microbiology 153 (2007) 1974-1980. (Pubitemid 46952527)
232. R. Meganathan, O. Kwon, Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q), in: R. Curtiss III, J.B. Kaper, C.L. Squires, P.D. Karp, F.C. Neidhardt, J.M. Slauch (Eds.), EcoSal, ASM Press, Washington DC, 2009.
233. D.J. Richardson, Bacterial respiration: a flexible process for a changing environment, Microbiology 146 (Pt 3) (2000) 551-571.
234. G. Unden, J. Bongaerts, Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors, Biochim. Biophys. Acta 1320 (1997) 217-234. (Pubitemid 27283364)
235. G. Unden, P. Dünnwald, The aerobic and anaerobic respiratory chain of Escherichia coli and Salmonella enterica: enzymes and energetics, in: R. Curtiss III, J.B. Kaper, C.L. Squires, P.D.Karp, F.C.Neidhardt, J.M. Slauch (Eds.), EcoSal, ASMPress,Washington, DC, 2008.
236. B. Soballe, R.K. Poole, Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management, Microbiology 145 (Pt 8) (1999) 1817-1830.
237. H.S. Kwan, E.L. Barrett, 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 (1983) 1147-1155. (Pubitemid 13023086)
238. U. Wissenbach, A. Kroger, G. Unden, The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli, Arch. Microbiol. 154 (1990) 60-66.
239. U. Wissenbach, D. Ternes, G. Unden, An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration, Arch. Microbiol. 158 (1992) 68-73.
240. R. Meganathan, Inability of men mutants of Escherichia coli to use trimethylamine- N-oxide as an electron acceptor, FEMS Microbiol. Lett. 24 (1984) 57-62. (Pubitemid 14039408)
241. C.R. Myers, J.M. Myers, Role of menaquinone in the reduction of fumarate, nitrate, iron(III) and manganese(IV) by Shewanella putrefaciens MR-1, FEMS Microbiol. Lett. 114 (1993) 215-222. (Pubitemid 23347769)
242. E.L. Barrett, M.A. Clark, Tetrathionate reduction and production of hydrogen sulfide from thiosulfate, Microbiol. Rev. 51 (1987) 192-205. (Pubitemid 17082510)
243. C. Novotny, F. Kapralek, Participation of quinone and cytochrome b in tetrathionate reductase respiratory chain of Citrobacter freundii, Biochem. J. 178 (1979) 237-240. (Pubitemid 9127600)
244. E.Maklashina, G. Cecchini, Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli, Arch. Biochem. Biophys. 369 (1999) 223-232. (Pubitemid 29455602)
245. H.S. Kwan, E.L. Barrett, Map locations and functions of Salmonella typhimurium men genes, J. Bacteriol. 159 (1984) 1090-1092. (Pubitemid 14048072)
246. L. Stoffels, M. Krehenbrink, B.C. Berks, G. Unden, Thiosulfate reduction in Salmonella enterica is driven by the proton motive force, J. Bacteriol. 194 (2012) 475-485.
247. K. Tyson, R. Metheringham, L. Griffiths, J. Cole, Characterisation of Escherichia coli K-12 mutants defective in formate-dependent nitrite reduction: essential roles for hemN and the menFDBCE operon, Arch. Microbiol. 168 (1997) 403-411. (Pubitemid 27455828)
248. T.H. Brondijk, D. Fiegen, D.J. Richardson, J.A. Cole, Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation, Mol. Microbiol. 44 (2002) 245-255. (Pubitemid 34429779)
249. L.C. Potter, J.A. Cole, Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12, Biochem. J. 344 (Pt 1) (1999) 69-76.
250. J. Simon,M. Sanger, S.C. Schuster, R. Gross, Electron transport to periplasmic nitrate reductase (NapA) of Wolinella succinogenes is independent of a NapC protein, Mol. Microbiol. 49 (2003) 69-79. (Pubitemid 36792004)
251. M. Kern, A.M. Mager, J. Simon, Role of individual nap gene cluster products in NapC-independent nitrate respiration of Wolinella succinogenes, Microbiology 153 (2007) 3739-3747. (Pubitemid 350168252)
252. G. Unden, Differential roles for menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their fnr-independent expression, Arch. Microbiol. 150 (1988) 499-503.
253. B. Soballe, R.K. Poole, Requirement for ubiquinone downstream of cytochrome(s) b in the oxygen-terminated respiratory chains of Escherichia coli K-12 revealed using a null mutant allele of ubiCA, Microbiology 144 (Pt 2) (1998) 361-373. (Pubitemid 28067741)
254. M.Y. Okamura, M.L. Paddock, M.S. Graige, G. Feher, Proton and electron transfer in bacterial reaction centers, Biochim. Biophys. Acta 1458 (2000) 148-163. (Pubitemid 30254256)
255. M. Sato-Watanabe, T. Mogi, H. Miyoshi, Y. Anraku, Characterization and functional role of the QH site of bo-type ubiquinol oxidase from Escherichia coli, Biochemistry 37 (1998) 5356-5361. (Pubitemid 28241916)
256. M. Sato-Watanabe, T.Mogi, T. Ogura, T. Kitagawa,H.Miyoshi,H. Iwamura, Y. Anraku, Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli, J. Biol. Chem. 269 (1994) 28908-28912. (Pubitemid 24366737)
257. L.L. Yap, M.T. Lin, H. Ouyang, R.I. Samoilova, S.A. Dikanov, R.B. Gennis, The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, Biochim. Biophys. Acta 1797 (2010) 1924-1932.
258. S.J. Marritt, T.G. Lowe, J. Bye, D.G. McMillan, L. Shi, J. Fredrickson, J. Zachara, D.J. Richardson, M.R. Cheesman, L.J. Jeuken, J.N. Butt, A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella, Biochem. J. 444 (2012) 465-474.
259. D.G.McMillan, S.J.Marritt, J.N. Butt, L.J. Jeuken,Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA, J. Biol. Chem. 287 (2012) 14215-14225.
260. M.G. Bertero, R.A. Rothery, N. Boroumand, M. Palak, F. Blasco, N. Ginet, J.H. Weiner, N.C. Strynadka, Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A, J. Biol. Chem. 280 (2005) 14836-14843. (Pubitemid 40562833)
261. R. Arias-Cartin, S. Grimaldi, P. Arnoux, B. Guigliarelli, A.Magalon, Cardiolipin binding in bacterial respiratory complexes: structural and functional implications, Biochim. Biophys. Acta 1817 (2012) 1937-1949.
262. R. Giordani, J. Buc, A. Cornish-Bowden, M.L. Cardenas, Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors-different reaction sites for menadiol and duroquinol, Eur. J. Biochem. 250 (1997) 567-577. (Pubitemid 28012701)
263. Z. Zhao, R.A. Rothery, J.H. Weiner, Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol, Biochemistry 42 (2003) 5403-5413. (Pubitemid 36560437)
264. R. Giordani, J. Buc, Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli, Eur. J. Biochem. 271 (2004) 2400-2407. (Pubitemid 38813570)
265. R.A. Rothery, J.H. Weiner, Interaction of an engineered 3Fe-4S cluster with a menaquinol binding site of Escherichia coli DMSO reductase, Biochemistry 35 (1996) 3247-3257. (Pubitemid 26082252)
266. Z. Zhao, J.H. Weiner, Interaction of 2-n-heptyl-4-hydroxyquinoline-N- oxide with dimethyl sulfoxide reductase of Escherichia coli, J. Biol. Chem. 273 (1998) 20758-20763. (Pubitemid 28385352)
267. P. Geijer, J.H. Weiner, Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli, Biochim. Biophys. Acta 1660 (2004) 66-74. (Pubitemid 38125232)
268. M.L. Rodrigues, K.A. Scott, M.S. Sansom, I.A. Pereira, M. Archer, Quinol oxidation by c-type cytochromes: structural characterization of the menaquinol binding site of NrfHA, J. Mol. Biol. 381 (2008) 341-350.
269. K. Zargar, C.W. Saltikov, Lysine-91 of the tetraheme c-type cytochrome CymA is essential for quinone interaction and arsenate respiration in Shewanella sp. strain ANA-3, Arch. Microbiol. 191 (2009) 797-806.
270. N. Fisher, P.R. Rich, Amotif for quinone binding sites in respiratory and photosynthetic systems, J. Mol. Biol. 296 (2000) 1153-1162.
271. V.W. Cheng, R.A. Rothery,M.G. Bertero, N.C. Strynadka, J.H.Weiner, Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase, Biochemistry 44 (2005) 8068-8077. (Pubitemid 40776668)
272. S. Grimaldi, R. Arias-Cartin, B. Guigliarelli, A. Magalon, unpublished results.
273. A. Hochman, A. Nissany, M. Amizur, Nitrate reduction and assimilation by a moderately halophilic, halotolerant bacterium BA-1, Biochim. Biophys. Acta 965 (1988) 82-89.
274. C. Moreno-Vivian, P. Cabello, M. Martinez-Luque, R. Blasco, F. Castillo, Prokaryotic nitrate reduction: molecular properties and functional distinction among bacterial nitrate reductases, J. Bacteriol. 181 (1999) 6573-6584. (Pubitemid 29517969)
275. E. Flores, J.E. Frias, L.M. Rubio, A. Herrero, Photosynthetic nitrate assimilation in cyanobacteria, Photosynth. Res. 83 (2005) 117-133. (Pubitemid 40374634)
276. M.J. Bonete, R.M. Martinez-Espinosa, C. Pire, B. Zafrilla, D.J. Richardson, Nitrogen metabolism in haloarchaea, Saline Syst. 4 (2008) 9.
277. I. Luque, A. Herrero, E. Flores, F.Madueno, Clustering of Genes Involved in Nitrate Assimilation in the Cyanobacterium Synechococcus, Mol.Gen.Genet 232 (1992) 7-11.
278. J.E. Frias, E. Flores, A. Herrero, Nitrate assimilation gene cluster from the heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120, J. Bacteriol. 179 (1997) 477-486. (Pubitemid 27030402)
279. Q. Wang, H. Li, A.F. Post, Nitrate assimilation genes of the marine diazotrophic, filamentous cyanobacterium Trichodesmium sp. strain WH9601, J. Bacteriol. 182 (2000) 1764-1767. (Pubitemid 30121145)
280. A.C.Martiny, S. Kathuria, P.M. Berube,Widespreadmetabolic potential for nitrite and nitrate assimilation among Prochlorococcus ecotypes, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 10787-10792.
281. J.E. Frias, E. Flores, Negative regulation of expression of the nitrate assimilation nirA operon in the heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120, J. Bacteriol. 192 (2010) 2769-2778.
282. M.Wyman, C. Bird, Lack of control of nitrite assimilation by ammoniumin an oceanic picocyanobacterium, Synechococcus sp. strainWH 8103, Appl. Environ.Microbiol. 73 (2007) 3028-3033. (Pubitemid 46718587)
283. Q.Wu, V. Stewart, NasFED proteins mediate assimilatory nitrate and nitrite transport in Klebsiella oxytoca (pneumoniae) M5al, J. Bacteriol. 180 (1998) 1311-1322. (Pubitemid 28119492)
284. J.C. Gutierrez, F. Ramos, L. Ortner, M. Tortolero, nasST, two genes involved in the induction of the assimilatory nitrite-nitrate reductase operon (nasAB) of Azotobacter vinelandii, Mol. Microbiol. 18 (1995) 579-591. (Pubitemid 26009114)
285. C. Pino, F. Olmo-Mira, P. Cabello, M. Martinez-Luque, F. Castillo, M.D. Roldan, C. Moreno-Vivian, The assimilatory nitrate reduction system of the phototrophic bacterium Rhodobacter capsulatus E1F1, Biochem. Soc. Trans. 34 (2006) 127-129. (Pubitemid 43235551)
286. J. Wang, G.P. Zhao, GlnR positively regulates nasA transcription in Streptomyces coelicolor, Biochem. Biophys. Res. Commun. 386 (2009) 77-81.
287. Z. Shao, J. Gao, X. Ding, J.Wang, J. Chiao, G. Zhao, Identification and functional analysis of a nitrate assimilation operon nasACKBDEF from Amycolatopsis mediterranei U32, Arch. Microbiol. 193 (2011) 463-477.
288. P. Cabello,M.D. Roldan, C.Moreno-Vivian,Nitrate reduction and the nitrogen cycle in archaea, Microbiology 150 (2004) 3527-3546. (Pubitemid 39545304)
289. R.M. Martinez-Espinosa, F.C. Marhuenda-Egea, M.J. Bonete, Assimilatory nitrate reductase from the haloarchaeon Haloferaxmediterranei: purification and characterisation, FEMS Microbiol. Lett. 204 (2001) 381-385. (Pubitemid 33145283)
290. R.M. Martinez-Espinosa, F.C. Marhuenda-Egea, M.J. Bonete, Purification and characterisation of a possible assimilatory nitrite reductase from the halophile archaeon Haloferax mediterranei, FEMS Microbiol. Lett. 196 (2001) 113-118. (Pubitemid 32232246)
291. B. Lledo, F.C. Marhuenda-Egea, R.M. Martinez-Espinosa, M.J. Bonete, Identification and transcriptional analysis of nitrate assimilation genes in the halophilic archaeon Haloferax mediterranei, Gene 361 (2005) 80-88. (Pubitemid 41506935)
292. R.M. Martinez-Espinosa, B. Lledo, F.C. Marhuenda-Egea, S. Diaz, M.J. Bonete, NO3 -/NO2 - assimilation in halophilic archaea: physiological analysis, nasA and nasD expressions, Extremophiles 13 (2009) 785-792.
293. S.H. Baek, G. Rajashekara, G.A. Splitter, J.P. Shapleigh, Denitrification genes regulate Brucella virulence in mice, J. Bacteriol. 186 (2004) 6025-6031. (Pubitemid 39186990)
294. N.E. Van Alst, K.F. Picardo, B.H. Iglewski, C.G. Haidaris, Nitrate sensing and metabolismmodulatemotility, biofilm formation, and virulence in Pseudomonas aeruginosa, Infect. Immun. 75 (2007) 3780-3790. (Pubitemid 47206275)
295. K.R. Barth, V.M. Isabella, V.L. Clark, Biochemical and genomic analysis of the denitrification pathway within the genus Neisseria, Microbiology 155 (2009) 4093-4103.
296. D. Richardson, G. Sawers, Structural biology. PMF through the redox loop, Science 295 (2002) 1842-1843. (Pubitemid 34214108)
297. H.D. Williams, J.E. Zlosnik, B. Ryall, Oxygen, cyanide and energy generation in the cystic fibrosis pathogen Pseudomonas aeruginosa, Adv. Microb. Physiol. 52 (2007) 1-71.
298. M. Aminuddin, D.J. Nicholas, Sulphide oxidation linked to the reduction of nitrate and nitrite in Thiobacillus denitrificans, Biochim. Biophys. Acta 325 (1973) 81-93.
299. H.R. Beller, P.S. Chain, T.E. Letain, A. Chakicherla, F.W. Larimer, P.M. Richardson,M.A. Coleman, A.P. Wood, D.P. Kelly, The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans, J. Bacteriol. 188 (2006) 1473-1488. (Pubitemid 43228681)
300. H.R. Beller, T.E. Letain, A. Chakicherla, S.R. Kane, T.C. Legler, M.A. Coleman, Whole-genome transcriptional analysis of chemolithoautotrophic thiosulfate oxidation by Thiobacillus denitrificans under aerobic versus denitrifying conditions, J. Bacteriol. 188 (2006) 7005-7015. (Pubitemid 44497913)
301. H.R. Beller, Anaerobic, nitrate-dependent oxidation of U(IV) oxide minerals by the chemolithoautotrophic bacterium Thiobacillus denitrificans, Appl. Environ. Microbiol. 71 (2005) 2170-2174. (Pubitemid 40546145)
302. H.R. Beller, T.C. Legler, F. Bourguet, T.E. Letain, S.R. Kane,M.A. Coleman, Identification of c-type cytochromes involved in anaerobic, bacterial U(IV) oxidation, Biodegradation 20 (2009) 45-53.
303. K.L. Straub, M. Benz, B. Schink, F. Widdel, Anaerobic, nitrate-dependent microbial oxidation of ferrous iron, Appl. Environ.Microbiol. 62 (1996) 1458-1460. (Pubitemid 26113236)
304. J. Bosch, K.Y. Lee, G. Jordan, K.W. Kim, R.U. Meckenstock, Anaerobic, nitratedependent oxidation of pyrite nanoparticles by Thiobacillus denitrificans, Environ. Sci. Technol. 46 (2012) 2095-2101.
305. S.E. Hoeft, J.S. Blum, J.F. Stolz, F.R. Tabita, B. Witte, G.M. King, J.M. Santini, R.S. Oremland, Alkalilimnicola ehrlichii sp. nov., a novel, arsenite-oxidizing haloalkaliphilic gammaproteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor, Int. J. Syst. Evol. Microbiol. 57 (2007) 504-512. (Pubitemid 46437862)
306. K.A. Weber, J. Pollock, K.A. Cole, S.M. O'Connor, L.A. Achenbach, J.D. Coates, Anaerobic nitrate-dependent iron(II) bio-oxidation by a novel lithoautotrophic betaproteobacterium, strain 2002, Appl. Environ. Microbiol. 72 (2006) 686-694.
307. L.J. Bird, V. Bonnefoy,D.K.Newman, Bioenergetic challenges ofmicrobial ironmetabolisms, Trends Microbiol. 19 (2011) 330-340.
308. M. Ilbert, V. Bonnefoy, Insight into the evolution of the iron oxidation pathways, Biochim. Biophys. Acta 1827 (2013) 161-175.
309. A. Chakraborty, E.E. Roden, J. Schieber, F. Picardal, Enhanced growth of Acidovorax sp. strain 2AN during nitrate-dependent Fe(II) oxidation in batch and continuous-flow systems, Appl. Environ.Microbiol. 77 (2011) 8548-8556.
310. H.K. Carlson, I.C. Clark, R.A. Melnyk, J.D. Coates, Toward a mechanistic understanding of anaerobic nitrate-dependent iron oxidation: balancing electron uptake and detoxification, Front. Microbiol. 3 (2012) 57.
311. T. Hoffmann, B. Troup, A. Szabo, C. Hungerer, D. Jahn, The anaerobic life of Bacillus subtilis: cloning of the genes encoding the respiratory nitrate reductase system, FEMS Microbiol. Lett. 131 (1995) 219-225.
312. M.M. Nakano, P. Zuber, Anaerobic growth of a "strict aerobe" (Bacillus subtilis), Annu. Rev. Microbiol. 52 (1998) 165-190.
313. H.I. Boshoff, C.E. Barry III, Tuberculosis - metabolism and respiration in the absence of growth, Nat. Rev. Microbiol. 3 (2005) 70-80. (Pubitemid 40028470)
314. M.M. Nakano, Y.P. Dailly, P. Zuber, D.P. Clark, Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth, J. Bacteriol. 179 (1997) 6749-6755. (Pubitemid 27465311)
315. E. Härtig, D. Jahn, Regulation of the anaerobic metabolism in Bacillus subtilis, Adv. Microb. Physiol. 61 (2012) 195-216.
316. M.P. Tan, P. Sequeira, W.W. Lin, W.Y. Phong, P. Cliff, S.H. Ng, B.H. Lee, L. Camacho, D. Schnappinger, S. Ehrt, T. Dick, K. Pethe, S. Alonso, Nitrate respiration protects hypoxic Mycobacterium tuberculosis against acid- and reactive nitrogen species stresses, PLoS One 5 (2010) e13356.
317. I. Weber, C. Fritz, S. Ruttkowski, A. Kreft, F.C. Bange, Anaerobic nitrate reductase (narGHJI) activity of Mycobacterium bovis BCG in vitro and its contribution to virulence in immunodeficient mice, Mol. Microbiol. 35 (2000) 1017-1025. (Pubitemid 30137772)
318. C.D. Sohaskey, Nitrate enhances the survival of Mycobacterium tuberculosis during inhibition of respiration, J. Bacteriol. 190 (2008) 2981-2986. (Pubitemid 351508198)
319. L.I. Hochstein, F. Lang, Purification and properties of a dissimilatory nitrate reductase from Haloferax denitrificans, Arch. Biochem. Biophys. 288 (1991) 380-385.
320. S. Bickelsandkötter, M. Ufer, Properties of a dissimilatory nitrate reductase from the halophilic archaeon Haloferax volcanii, Z. Naturforsch. C Biosci. 50 (1995) 365-372.
321. B. Lledo, R.M. Martinez-Espinosa, F.C. Marhuenda-Egea, M.J. Bonete, Respiratory nitrate reductase from haloarchaeon Haloferax mediterranei: biochemical and genetic analysis, Biochim. Biophys. Acta 1674 (2004) 50-59. (Pubitemid 39165815)
322. K. Yoshimatsu, T. Sakurai, T. Fujiwara, Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui, FEBS Lett. 470 (2000) 216-220. (Pubitemid 30151099)
323. K. Yoshimatsu, O. Araya, T. Fujiwara, Haloarcula marismortui cytochrome b-561 is encoded by the narC gene in the dissimilatory nitrate reductase operon, Extremophiles 11 (2007) 41-47. (Pubitemid 46089628)
324. M. Schutz,M. Brugna, E. Lebrun, F. Baymann, R.Huber, K.O. Stetter, G.Hauska, R. Toci, D. Lemesle-Meunier, P. Tron,C. Schmidt,W. Nitschke, Early evolution of cytochrome bc complexes, J. Mol. Biol. 300 (2000) 663-675.
325. P. Volkl, R. Huber, E. Drobner, R. Rachel, S. Burggraf, A. Trincone, K.O. Stetter, Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum, Appl. Environ. Microbiol. 59 (1993) 2918-2926.
326. L.F. Feinberg, J.F. Holden, Characterization of dissimilatory Fe(III) versus NO3 - reduction in the hyperthermophilic archaeon Pyrobaculum aerophilum, J. Bacteriol. 188 (2006) 525-531. (Pubitemid 43100541)
327. A.E. Cozen, M.T. Weirauch, K.S. Pollard, D.L. Bernick, J.M. Stuart, T.M. Lowe, Transcriptional map of respiratory versatility in the hyperthermophilic crenarchaeon Pyrobaculum aerophilum, J. Bacteriol. 191 (2009) 782-794.
328. S. Ramirez-Arcos, L.A. Fernandez-Herrero, J. Berenguer, A thermophilic nitrate reductase is responsible for the strain specific anaerobic growth of Thermus thermophilus HB8, Biochim. Biophys. Acta 1396 (1998) 215-227. (Pubitemid 28150183)
329. F. Cava, O. Zafra, A.Magalon, F. Blasco, J. Berenguer, A newtype of NADH dehydrogenase specific for nitrate respiration in the extreme thermophile Thermus thermophilus, J. Biol. Chem. 279 (2004) 45369-45378. (Pubitemid 39491520)
330. F. Cava, O. Zafra, M.S. da Costa, J. Berenguer, The role of the nitrate respiration element of Thermus thermophilus in the control and activity of the denitrification apparatus, Environ. Microbiol. 10 (2008) 522-533.
331. D. Heintz, S. Gallien, S. Wischgoll, A.K. Ullmann, C. Schaeffer, A.K. Kretzschmar, A. van Dorsselaer, M. Boll, Differential membrane proteome analysis reveals novel proteins involved in the degradation of aromatic compounds in Geobacter metallireducens, Mol. Cell. Proteomics 8 (2009) 2159-2169.
332. K.T. Finneran, M.E. Housewright, D.R. Lovley, Multiple influences of nitrate on uranium solubility during bioremediation of uranium-contaminated subsurface sediments, Environ. Microbiol. 4 (2002) 510-516.
333. J.O. Lundberg, E. Weitzberg, J.A. Cole, N. Benjamin, Nitrate, bacteria and human health, Nat. Rev. Microbiol. 2 (2004) 593-602. (Pubitemid 39200033)
334. C.E. Vine, J.A. Cole, Unresolved sources, sinks, and pathways for the recovery of enteric bacteria from nitrosative stress, FEMS Microbiol. Lett. 325 (2011) 99-107.
335. D. Seth, A. Hausladen, Y.J.Wang, J.S. Stamler, Endogenous protein S-nitrosylation in E. coli: regulation by OxyR, Science 336 (2012) 470-473.
336. A. Arkenberg, S. Runkel, D.J. Richardson, G. Rowley, The production and detoxification of a potent cytotoxin, nitric oxide, by pathogenic enteric bacteria, Biochem. Soc. Trans. 39 (2011) 1876-1879.
337. A. Trivedi, N. Singh, S.A. Bhat, P. Gupta, A. Kumar, Redox biology of tuberculosis pathogenesis, Adv. Microb. Physiol. 60 (2012) 263-324.
338. C.A. Lopez, S.E. Winter, F. Rivera-Chavez, M.N. Xavier, V. Poon, S.P. Nuccio, R.M. Tsolis, A.J. Baumler, Phage-mediated acquisition of a type III secreted effector protein boosts growth of Salmonella by nitrate respiration, MBio 3 (2012).
339. W.G. Zumft, Cell biology and molecular basis of denitrification, Microbiol. Mol. Biol. Rev. 61 (1997) 533-616. (Pubitemid 28006959)
340. D.J. Richardson, B.C. Berks,D.A. Russell, S. Spiro, C.J. Taylor, Functional, biochemical and genetic diversity of prokaryotic nitrate reductases, Cell. Mol. Life Sci. 58 (2001) 165-178. (Pubitemid 32217349)
341. L. Potter, H. Angove, D. Richardson, J. Cole, Nitrate reduction in the periplasm of Gram-negative bacteria, Adv. Microb. Physiol. 45 (2001) 51-112. (Pubitemid 32612190)
342. H.P. Liu, S. Takio, T. Satoh, I. Yamamoto, Involvement in denitrification of the napKEFDABC genes encoding the periplasmic nitrate reductase system in the denitrifying phototrophic bacterium Rhodobacter sphaeroides f. sp. denitrificans, Biosci. Biotechnol. Biochem. 63 (1999) 530-536. (Pubitemid 129555500)
343. L. Bedzyk, T. Wang, R.W. Ye, The periplasmic nitrate reductase in Pseudomonas sp. strain G-179 catalyzes the first step of denitrification, J. Bacteriol. 181 (1999) 2802-2806. (Pubitemid 29211096)
344. D.J. Richardson, G.F. King, D.J. Kelly, A.G.McEwan, S.J. Ferguson, J.B. Jackson, The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on proprionate or butyrate, Arch. Microbiol. 150 (1988) 131-137.
345. D.J. Richardson, S.J. Ferguson, The influence of carbon substrate on the activity of the periplasmic nitrate reductase in aerobically grown Thiosphaera pantotropha, Arch. Microbiol. 157 (1992) 535-537.
346. M.D. Roldan, F. Reyes, C. Morenovivian, F. Castillo, Chlorate and nitrate reduction in the phototrophic bacteria Rhodobacter capsulatus and Rhodobacter sphaeroides, Curr. Microbiol. 29 (1994) 241-245. (Pubitemid 24271164)
347. H.J. Sears, S. Spiro, D.J. Richardson, Effect of carbon substrate and aeration on nitrate reduction and expression of the periplasmic and membrane-bound nitrate reductases in carbon-limited continuous cultures of Paracoccus denitrificans Pd1222, Microbiology-(UK) 143 (1997) 3767-3774. (Pubitemid 28004609)
348. H.J. Sears, G. Sawers, B.C. Berks, S.J. Ferguson, D.J. Richardson, Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates, Microbiology 146 (Pt 11) (2000) 2977-2985.
349. M. Gavira,M.D. Roldan, F. Castillo, C.Moreno-Vivian, Regulation of nap gene expression and periplasmic nitrate reductase activity in the phototrophic bacterium Rhodobacter sphaeroides DSM158, J. Bacteriol. 184 (2002) 1693-1702. (Pubitemid 34188221)
350. L.C. Potter, P. Millington, L. Griffiths, G.H. Thomas, J.A. Cole, 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) (1999) 77-84.
351. V. Stewart, Y. Lu, A.J. Darwin, Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12, J. Bacteriol. 184 (2002) 1314-1323. (Pubitemid 34157553)
352. M.S. Pittman, D.J. Kelly, Electron transport through nitrate and nitrite reductases in Campylobacter jejuni, Biochem. Soc. Trans. 33 (2005) 190-192. (Pubitemid 40313798)
353. M. Kern, J. Simon, Electron transport chains and bioenergetics of respiratory nitrogen metabolism in Wolinella succinogenes and other Epsilonproteobacteria, Biochim. Biophys. Acta 1787 (2009) 646-656.
354. J.J. Rowe, T. Ubbink-Kok, D. Molenaar, W.N. Konings, A.J. Driessen, NarK is a nitrite-extrusion system involved in anaerobic nitrate respiration by Escherichia coli, Mol. Microbiol. 12 (1994) 579-586. (Pubitemid 24159600)
355. N.J. Wood, T. Alizadeh, D.J. Richardson, S.J. Ferguson, J.W. Moir, Two domains of a dual-function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus, Mol. Microbiol. 44 (2002) 157-170. (Pubitemid 34429772)
356. W. Jia, N. Tovell, S. Clegg, M. Trimmer, J. Cole, A single channel for nitrate uptake, nitrite export and nitrite uptake by Escherichia coli NarU and a role for NirC in nitrite export and uptake, Biochem. J. 417 (2009) 297-304.
357. J. Simon, Enzymology and bioenergetics of respiratory nitrite ammonification, FEMS Microbiol. Rev. 26 (2002) 285-309.
358. M.J. Sellars, S.J. Hall, D.J. Kelly, Growth of Campylobacter jejuni supported by respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide requires oxygen, J. Bacteriol. 184 (2002) 4187-4196. (Pubitemid 34774299)
359. R.A. Weingarten, J.L. Grimes, J.W. Olson, Role of Campylobacter jejuni respiratory oxidases and reductases in host colonization, Appl. Environ. Microbiol. 74 (2008) 1367-1375. (Pubitemid 351358431)
360. C. Cruz-Garcia, A.E. Murray, J.A. Klappenbach, V. Stewart, J.M. Tiedje, Respiratory nitrate ammonification by Shewanella oneidensis MR-1, J. Bacteriol. 189 (2007) 656-662. (Pubitemid 46106399)
361. H. Gao, Z.K. Yang, S. Barua, S.B. Reed, M.F. Romine, K.H. Nealson, J.K. Fredrickson, J.M. Tiedje, J. Zhou, Reduction of nitrate in Shewanella oneidensis depends on atypical NAP and NRF systems with NapB as a preferred electron transport protein from CymA to NapA, ISME J. 3 (2009) 966-976.
362. A. Marietou, D. Richardson, J. Cole, S. Mohan, Nitrate reduction by Desulfovibrio desulfuricans: a periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM, FEMS Microbiol. Lett. 248 (2005) 217-225. (Pubitemid 40942131)
363. R.A. Siddiqui, U. Warnecke-Eberz, A. Hengsberger, B. Schneider, S. Kostka, B. Friedrich, Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16, J. Bacteriol. 175 (1993) 5867-5876. (Pubitemid 23277434)
364. Y. Li, E. Katzmann, S. Borg, D. Schuler, The periplasmic nitrate reductase nap is required for anaerobic growth and involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense, J. Bacteriol. 194 (2012) 4847-4856.
365. F. Reyes, M. Gavira, F. Castillo, C. Moreno-Vivian, Periplasmic nitrate-reducing system of the phototrophic bacterium Rhodobacter sphaeroides DSM 158: transcriptional and mutational analysis of the napKEFDABC gene cluster, Biochem. J. 331 (Pt 3) (1998) 897-904. (Pubitemid 28211915)
366. H.P. Koops, A. Pommerening-Roser, Distribution and ecophysiology of the nitrifying bacteria emphasizing cultured species, FEMS Microbiol. Ecol. 37 (2001) 1-9. (Pubitemid 32800676)
367. S.E. Vlaeminck, A.G. Hay, L.Maignien,W. Verstraete, In quest of the nitrogen oxidizing prokaryotes of the early Earth, Environ. Microbiol. 13 (2011) 283-295.
368. K. Kirstein, E. Bock, Close genetic relationship between Nitrobacter hamburgensis nitrite oxidoreductase and Escherichia coli nitrate reductases, Arch. Microbiol. 160 (1993) 447-453. (Pubitemid 23334012)
369. H. Sundermeyer-klinger, W. Meyer, B. Warninghoff, E. Bock, Membrane-bound nitrite oxidoreductase of nitrobacter - evidence for a nitrate reductase system, Arch. Microbiol. 140 (1984) 153-158. (Pubitemid 15181734)
370. A. Freitag, M. Rudert, E. Bock, Growth of Nitrobacter by dissimilatoric nitrate reduction, FEMS Microbiol. Lett. 48 (1987) 105-109.
371. E. Bock, P.A. Wilderer, A. Freitag, Growth of Nitrobacter in the absence of dissolved oxygen,Water Res. 22 (1988) 245-250. (Pubitemid 18050113)
372. A. Teske, E. Alm, J.M. Regan, S. Toze, B.E. Rittmann, D.A. Stahl, Evolutionary relationships among ammonia- and nitrite-oxidizing bacteria, J. Bacteriol. 176 (1994) 6623-6630. (Pubitemid 24338076)
373. T. Yamanaka, Y. Fukumori, The nitrite oxidizing system of Nitrobacter winogradskyi, FEMS Microbiol. Rev. 4 (1988) 259-270.
374. L. van Niftrik, M.S. Jetten, Anaerobic ammonium-oxidizing bacteria: unique microorganisms with exceptional properties, Microbiol. Mol. Biol. Rev. 76 (2012) 585-596.
375. M. Strous, E. Pelletier, S. Mangenot, T. Rattei, A. Lehner, M.W. Taylor, M. Horn, H. Daims, D. Bartol-Mavel, P. Wincker, V. Barbe, N. Fonknechten, D. Vallenet, B. Segurens, C. Schenowitz-Truong, C. Medigue, A. Collingro, B. Snel, B.E. Dutilh, H.J. Op den Camp, C. van der Drift, I. Cirpus, K.T. van de Pas-Schoonen, H.R. Harhangi, L. van Niftrik, M. Schmid, J. Keltjens, J. van de Vossenberg, B. Kartal, H. Meier, D. Frishman, M.A. Huynen, H.W. Mewes, J. Weissenbach, M.S. Jetten, M. Wagner, D. Le Paslier, Deciphering the evolution and metabolism of an Anammox bacterium from a community genome, Nature 440 (2006) 790-794.
376. B. Kartal,W.J.Maalcke, N.M. de Almeida, I. Cirpus, J. Gloerich,W. Geerts, H.J. Op den Camp, H.R. Harhangi, E.M. Janssen-Megens, K.J. Francoijs, H.G. Stunnenberg, J.T. Keltjens, M.S. Jetten,M. Strous, Molecular mechanism of anaerobic ammonium oxidation, Nature 479 (2011) 127-130.
377. B. Kartal, M.M. Kuypers, G. Lavik, J. Schalk, H.J. Op den Camp, M.S. Jetten, M. Strous, Anammox bacteria disguised as denitrifiers: nitrate reduction to dinitrogen gas via nitrite and ammonium, Environ. Microbiol. 9 (2007) 635-642.
378. J. van de Vossenberg, J.E. Rattray, W. Geerts, B. Kartal, L. van Niftrik, E.G. van Donselaar, J.S. Sinninghe Damste, M. Strous, M.S. Jetten, Enrichment and characterization of marine anammox bacteria associated with global nitrogen gas production, Environ. Microbiol. 10 (2008) 3120-3129.
379. N.M. de Almeida, W.J. Maalcke, J.T. Keltjens, M.S. Jetten, B. Kartal, Proteins and protein complexes involved in the biochemical reactions of anaerobic ammonium-oxidizing bacteria, Biochem. Soc. Trans. 39 (2011) 303-308.
380. J.F. Heidelberg, I.T. Paulsen, K.E. Nelson, E.J. Gaidos,W.C. Nelson, T.D. Read, J.A. Eisen, R. Seshadri,N.Ward, B.Methe, R.A.Clayton, T.Meyer, A. Tsapin, J.Scott,M.Beanan, L. Brinkac, S. Daugherty, R.T. DeBoy, R.J. Dodson, A.S. Durkin, D.H. Haft, J.F. Kolonay, R. Madupu, J.D. Peterson, L.A. Umayam, O. White, A.M. Wolf, J. Vamathevan, J. Weidman, M. Impraim, K. Lee, K. Berry, C. Lee, J. Mueller, H. Khouri, J. Gill, T.R. Utterback, L.A. McDonald, T.V. Feldblyum, H.O. Smith, J.C. Venter, K.H. Nealson, C.M. Fraser, Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis, Nat. Biotechnol. 20 (2002) 1118-1123. (Pubitemid 35285440)
381. I. Yamamoto,M. Ishimoto, Anaerobic growth of Escherichia coli on formate by reduction of nitrate, fumarate, and trimethylamine N-oxide, Z. Allg. Mikrobiol. 17 (1977) 235-242. (Pubitemid 8071683)
382. A.G. McEwan, S.J. Ferguson, J.B. Jackson, Electron flow to dimethylsulphoxide or trimethylamine-N-oxide generates a membrane potential in Rhodopseudomonas capsulata, Arch. Microbiol. 136 (1983) 300-305. (Pubitemid 14191510)
383. R. Hedderich, O. Klimmek, A. Kröger, R. Dirmeier, M. Keller, K.O. Stetter, Anaerobic respiration with elemental sulfur and with disulfides, FEMS Microbiol. Rev. 22 (1999) 353-381.
384. A. Kletzin, T. Urich, F. Muller, T.M. Bandeiras, C.M. Gomes, Dissimilatory oxidation and reduction of elemental sulfur in thermophilic archaea, J. Bioenerg. Biomembr. 36 (2004) 77-91. (Pubitemid 38500762)
385. G.D. Fauque, L.L. Barton, Hemoproteins in dissimilatory sulfate- and sulfur-reducing prokaryotes, Adv. Microb. Physiol. 60 (2012) 1-90.
386. M. Guiral, L. Prunetti, C. Aussignargues, A. Ciaccafava, P. Infossi, M. Ilbert, E. Lojou, M.T. Giudici-Orticoni, The hyperthermophilic bacterium Aquifex aeolicus: from respiratory pathways to extremely resistant enzymes and biotechnological applications, Adv. Microb. Physiol. 61 (2012) 125-194.
387. I. Schroder, A. Kroger, J.M. Macy, Isolation of the sulfur reductase and reconstitution of the sulfur respiration of Wolinella succinogenes, Arch. Microbiol. 149 (1988) 572-579.
388. T. Krafft, M. Bokranz, O. Klimmek, I. Schroder, F. Fahrenholz, E. Kojro, A. Kroger, Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase, Eur. J. Biochem. 206 (1992) 503-510.
389. T. Krafft, R. Gross, A. Kroger, The function ofWolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor, Eur. J. Biochem. 230 (1995) 601-606.
390. J.M. Macy, I. Schroder, R.K. Thauer, A. Kroger, Growth of Wolinella succinogenes on H2S plus fumarate and on formate plus sulfur as energy sources, Arch. Microbiol. 144 (1986) 147-150. (Pubitemid 16131222)
391. O. Klimmek, A. Kroger, R. Steudel, G. Holdt, Growth of Wolinella succinogenes with polysulfide as terminal acceptor of phosphorylative electron transport, Arch. Microbiol. 155 (1991) 177-182.
392. M. Yamamoto, S. Nakagawa, S. Shimamura, K. Takai, K. Horikoshi, Molecular characterization of inorganic sulfur-compound metabolism in the deep-sea epsilonproteobacterium Sulfurovum sp. NBC37-1, Environ. Microbiol. 12 (2010) 1144-1153.
393. S. Laska, F. Lottspeich, A. Kletzin, Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens,Microbiology 149 (2003) 2357-2371. (Pubitemid 37160712)
394. A.Magalon,R. Arias-Cartin,A.Walburger, Supramolecular organization in prokaryotic respiratory systems, in: R.K. Poole (Ed.), Adv Microb Physiol, Academic press, 2012, pp. 217-266.
395. A. Jankielewicz, O. Klimmek, A. Kröger, The electron transfer from hydrogenase and formate dehydrogenase to polysulfide reductase in the membrane of Wolinella succinogenes, Biochim. Biophys. Acta 1231 (1995) 157-162.
396. G. Lenaz, M.L. Genova, Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject, Antioxid. Redox Signal. 12 (2010) 961-1008.
397. K. Yokoyama, T. Oshima, M. Yoshida, Thermus thermophilus membrane-associate ATPase: indication of a eubacterial V-type ATPase, J. Biol. Chem. 265 (1990) 21946-21950. (Pubitemid 120014247)
398. D.P.Moser, K.H. Nealson, Growth of the facultative anaerobe Shewanella putrefaciens by elemental sulfur reduction, Appl. Environ. Microbiol. 62 (1996) 2100-2105. (Pubitemid 26169007)
399. J.L. Burns, T.J. DiChristina, Anaerobic respiration of elemental sulfur and thiosulfate by Shewanella oneidensis MR-1 requires psrA, a homolog of the phsA gene of Salmonella enterica serovar typhimurium LT2, Appl. Environ. Microbiol. 75 (2009) 5209-5217.
400. A.P. Hinsley, B.C. Berks, Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica, Microbiology 148 (2002) 3631-3638. (Pubitemid 35414472)
401. F. Fischer,W. Zillig, K.O. Stetter, G. Schreiber, Chemolithoautotrophic metabolism of anaerobic extremely thermophilic archaebacteria, Nature 301 (1983) 511-513. (Pubitemid 13160568)
402. L.F. Feinberg, R. Srikanth, R.W. Vachet, J.F. Holden, Constraints on anaerobic respiration in the hyperthermophilic Archaea Pyrobaculum islandicum and Pyrobaculum aerophilum, Appl. Environ.Microbiol. 74 (2008) 396-402.
403. S.T. Fitz-Gibbon, H. Ladner, U.J. Kim, K.O. Stetter, M.I. Simon, J.H. Miller, Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum, Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 984-989. (Pubitemid 34106622)
404. P.P. Chan, A.D. Holmes, A.M. Smith, D. Tran, T.M. Lowe, The UCSC Archaeal genome browser: 2012 update, Nucleic Acids Res. 40 (2012) D646-D652.
405. S.E.Winter, P. Thiennimitr,M.G.Winter, B.P. Butler, D.L. Huseby, R.W. Crawford, J.M. Russell, C.L. Bevins, L.G. Adams, R.M. Tsolis, J.R. Roth, A.J. Baumler, Gut inflammation provides a respiratory electron acceptor for Salmonella, Nature 467 (2010) 426-429.
406. S.P. Hanlon, R.A. Holt, G.R. Moore, A.G. McEwan, Isolation and characterization of a strain of Rhodobacter sulfidophilus: a bacterium which grows autotrophically with dimethylsulfide as electron donor, Microbiology 140 (1994) 6.
407. J.H. Weiner, R.A. Rothery, D. Sambasivarao, C.A. Trieber, Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli, Biochim. Biophys. Acta 1102 (1992) 1-18.
408. D.A. Saffarini, S.L. Blumerman, K.J. Mansoorabadi, Role of menaquinones in Fe(III) reduction by membrane fractions of Shewanella putrefaciens, J. Bacteriol. 184 (2002) 846-848. (Pubitemid 34150233)
409. C.Gruber, A. Legat,M. Pfaffenhuemer, C. Radax, G.Weidler, H.J. Busse, H. Stan-Lotter, Halobacterium noricense sp. nov., an archaeal isolate from a bore core of an alpine Permian salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. salinarum and emended description of H. salinarum, Extremophiles 8 (2004) 431-439.
410. A. Oren, H.G. Trüper, Anaerobic growth of halophilic archaebacteria by reduction of dimethylsulfoxide and trimethylamine N-oxide, FEMS Microbiol. Lett. 70 (1990) 33-36. (Pubitemid 20211751)
411. S.L. McCrindle, U. Kappler, A.G. McEwan, Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration, Adv. Microb. Physiol. 50 (2005) 147-198. (Pubitemid 41428407)
412. G. Sawers, The hydrogenases and formate dehydrogenases of Escherichia coli, Antonie Van Leeuwenhoek 66 (1994) 57-88.
413. S.M. da Silva, I. Pacheco, I.A. Pereira, Electron transfer between periplasmic formate dehydrogenase and cytochromes c in Desulfovibrio desulfuricans ATCC 27774, J. Biol. Inorg. Chem. 17 (2012) 831-838.
414. D.J. Steenkamp, H.D. Peck Jr., Proton translocation associated with nitrite respiration in Desulfovibrio desulfuricans, J. Biol. Chem. 256 (1981) 5450-5458. (Pubitemid 11035381)
415. L.L. Barton, J. LeGall, J.M. Odom, H.D. Peck Jr., Energy coupling to nitrite respiration in the sulfate-reducing bacterium Desulfovibrio gigas, J. Bacteriol. 153 (1983) 867-871. (Pubitemid 13052812)
416. D.R. Lovley, D.E. Holmes, K.P. Nevin, Dissimilatory Fe(III) and Mn(IV) reduction, Adv. Microb. Physiol. 49 (2004) 219-286. (Pubitemid 39424008)
417. D.R. Lovley, T. Ueki, T. Zhang, N.S. Malvankar, P.M. Shrestha, K.A. Flanagan, M. Aklujkar, J.E. Butler, L. Giloteaux, A.E. Rotaru, D.E. Holmes, A.E. Franks, R. Orellana, C. Risso, K.P. Nevin, Geobacter: the microbe electric's physiology, ecology, and practical applications, Adv. Microb. Physiol. 59 (2011) 1-100.
418. C.R. Myers, J.M. Myers, Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1, J. Bacteriol. 179 (1997) 1143-1152. (Pubitemid 27076577)
419. L. Shi, T.C. Squier, J.M. Zachara, J.K. Fredrickson, Respiration of metal (hydr)oxides by Shewanella and Geobacter: a key role for multihaem c-type cytochromes, Mol. Microbiol. 65 (2007) 12-20. (Pubitemid 46934494)
420. A.Niggemyer, S. Spring, E. Stackebrandt, R.F. Rosenzweig, Isolation and characterization of a novel As(V)-reducing bacterium: implications for arsenic mobilization and the genus Desulfitobacterium, Appl. Environ. Microbiol. 67 (2001) 5568-5580. (Pubitemid 33640991)
421. K.C. Costa, P.M. Wong, T. Wang, T.J. Lie, J.A. Dodsworth, I. Swanson, J.A. Burn, M. Hackett, J.A. Leigh, Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase, Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 11050-11055.
422. M. Karrasch, G. Borner, M. Enssle, R.K. Thauer, Formylmethanofuran dehydrogenase from methanogenic bacteria, a molybdoenzyme, FEBS Lett. 253 (1989) 226-230.
423. M. Karrasch, G. Borner, M. Enssle, R.K. Thauer, The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor, Eur. J. Biochem. 194 (1990) 367-372.
424. M. Karrasch, G. Borner, R.K. Thauer, The molybdenum cofactor of formylmethanofuran dehydrogenase from Methanosarcina barkeri is a molybdopterin guanine dinucleotide, FEBS Lett. 274 (1990) 48-52. (Pubitemid 20378118)
425. P.A. Bertram, R.K. Thauer, Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum, Eur. J. Biochem. 226 (1994) 811-818.
426. A. Hochheimer, R.A. Schmitz, R.K. Thauer, R. Hedderich, The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide, Eur. J. Biochem. 234 (1995) 910-920. (Pubitemid 26023445)
427. A. Hochheimer, D. Linder, R.K. Thauer, R. Hedderich, The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation, Eur. J. Biochem. 242 (1996) 156-162. (Pubitemid 26386367)
428. B. Ezraty, J. Bos, F. Barras, L. Aussel,Methionine sulfoxide reduction and assimilation in Escherichia coli: new role for the biotin sulfoxide reductase BisC, J. Bacteriol. 187 (2005) 231-237. (Pubitemid 40024199)
429. V.V. Pollock, M.J. Barber, Kinetic and mechanistic properties of biotin sulfoxide reductase, Biochemistry 40 (2001) 1430-1440. (Pubitemid 32142905)
430. D.E. Pierson, A. Campbell, Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli, J. Bacteriol. 172 (1990) 2194-2198. (Pubitemid 20112050)
431. A. Brune, B. Schink, Pyrogallol-to-phloroglucinol conversion and other hydroxyltransfer reactions catalyzed by cell extracts of Pelobacter acidigallici, J. Bacteriol. 172 (1990) 1070-1076. (Pubitemid 20070421)
432. P.I. Darley, J.A. Hellstern, J.I. Medina-Bellver, S. Marques, B. Schink, B. Philipp, Heterologous expression and identification of the genes involved in anaerobic degradation of 1,3-dihydroxybenzene (resorcinol) in Azoarcus anaerobius, J. Bacteriol. 189 (2007) 3824-3833. (Pubitemid 46740180)
433. S. Schnell, F. Bak,N. Pfennig, Anaerobic degradation of aniline and dihydroxybenzenes by newly isolated sulfate-reducing bacteria and description of Desulfobacterium anilini, Arch. Microbiol. 152 (1989) 556-563.
434. A. Tschech, B. Schink, Fermentative degradation of resorcinol and resorcylic acids, Arch. Microbiol. 143 (1985) 8.
435. C. Kluge, A. Tschech, G. Fuchs, Anaerobic metabolism of resorcyclic acids (m-dihydroxybenzoic acids) and resorcinol (1,3-benzenediol) in a fermenting and in a denitrifying bacterium, Arch. Microbiol. 155 (1990) 7.
436. N. Springer, W. Ludwig, B. Philipp, B. Schink, Azoarcus anaerobius sp. nov., a resorcinol-degrading, strictly anaerobic, denitrifying bacterium, Int. J. Syst. Bacteriol. 48 (Pt 3) (1998) 953-956. (Pubitemid 28394678)
437. B. Philipp, B. Schink, Evidence of two oxidative reaction steps initiating anaerobic degradation of resorcinol (1,3-dihydroxybenzene) by the denitrifying bacterium Azoarcus anaerobius, J. Bacteriol. 180 (1998) 3644-3649. (Pubitemid 29115095)
438. H.A. Ball, H.A. Johnson, M. Reinhard, A.M. Spormann, Initial reactions in anaerobic ethylbenzene oxidation by a denitrifying bacterium, strain EB1, J. Bacteriol. 178 (1996) 5755-5761. (Pubitemid 26327678)
439. O. Kniemeyer, J. Heider, (S)-1-phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme of anaerobic ethylbenzene catabolism, Arch. Microbiol. 176 (2001) 129-135. (Pubitemid 32692653)
440. O. Kniemeyer, J. Heider, Ethylbenzene dehydrogenase, a novel hydrocarbonoxidizing molybdenum/iron-sulfur/heme enzyme, J. Biol. Chem. 276 (2001) 21381-21386.
441. A.S. Backlund, J. Bohlin, N. Gustavsson, T. Nilsson, Periplasmic c
442. M.K. Saiki, T.P. Lowe, Selenium in aquatic organisms from subsurface agricultural drainage water, San Joaquin Valley, California, Arch. Environ. Contam. Toxicol. 16 (1987) 657-670. (Pubitemid 17149463)
443. M. Bebien, J. Kirsch, V. Mejean, A. Vermeglio, Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli, Microbiology 148 (2002) 3865-3872. (Pubitemid 36097448)
444. H. Ridley, C.A. Watts, D.J. Richardson, C.S. Butler, Resolution of distinct membranebound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions, Appl. Environ. Microbiol. 72 (2006) 5173-5180.
445. D. Ahmann, A.L. Roberts, L.R. Krumholz, F.M. Morel, Microbe grows by reducing arsenic, Nature 371 (1994) 750.
446. W. Sun, R. Sierra-Alvarez, L. Milner, J.A. Field, Anaerobic oxidation of arsenite linked to chlorate reduction, Appl. Environ. Microbiol. 76 (2010) 6804-6811.
447. T.R. Kulp, S.E. Hoeft, M. Asao, M.T. Madigan, J.T. Hollibaugh, J.C. Fisher, J.F. Stolz, C.W. Culbertson, L.G. Miller, R.S. Oremland, Arsenic(III) fuels anoxygenic photosynthesis in hot spring biofilms from Mono Lake, California, Science 321 (2008) 967-970.
448. C. Richey, P. Chovanec, S.E. Hoeft, R.S. Oremland, P. Basu, J.F. Stolz, Respiratory arsenate reductase as a bidirectional enzyme, Biochem. Biophys. Res. Commun. 382 (2009) 298-302.
449. E.D. Rhine, S.M. Ni Chadhain, G.J. Zylstra, L.Y. Young, The arsenite oxidase genes (aroAB) in novel chemoautotrophic arsenite oxidizers, Biochem. Biophys. Res. Commun. 354 (2007) 662-667. (Pubitemid 46186235)
450. W. Sun, R. Sierra-Alvarez, L. Milner, R. Oremland, J.A. Field, Arsenite and ferrous iron oxidation linked to chemolithotrophic denitrification for the immobilization of arsenic in anoxic environments, Environ. Sci. Technol. 43 (2009) 6585-6591.
451. J.C. Fisher, J.T. Hollibaugh, Selenate-dependent anaerobic arsenite oxidation by a bacterium from Mono Lake, California, Appl. Environ. Microbiol. 74 (2008) 2588-2594. (Pubitemid 351632588)
452. P. Mitchell, Chemiosmotic coupling in oxidative and photosynthetic phosphorylation, Biol. Rev. Camb. Philos. Soc. 41 (1966) 445-502.
453. B. Frangioni, B. Guigliarelli, C. Iobbi-Nivol, Unpublished results.
454. P.J. Simpson, A.A. McKinzie, R. Codd, Resolution of two native monomeric 90 kDa nitrate reductase active proteins from Shewanella gelidimarina and the sequence of two napA genes, Biochem. Biophys. Res. Commun. 398 (2010) 13-18.
455. M.J. Barber, H.D. May, J.G. Ferry, Inactivation of formate dehydrogenase from Methanobacterium-formicicum by cyanide, Biochemistry 25 (1986) 8150-8155. (Pubitemid 17233512)
456. R. Gangeswaran, D.J. Lowe, R.R. Eady, Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii, Biochem. J. 289 (Pt 2) (1993) 335-342. (Pubitemid 23042037)
457. K.R. Hoke, N. Cobb, F.A. Armstrong, R. Hille, Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center, Biochemistry 43 (2004) 1667-1674. (Pubitemid 38200573)
458. C.A. Libeu, M. Kukimoto, M. Nishiyama, S. Horinouchi, E.T. Adman, Site-directed mutants of pseudoazurin: explanation of increased redox potentials from X-ray structures and from calculation of redox potential differences, Biochemistry 36 (1997) 13160-13179. (Pubitemid 27473360)
459. N.L. Creevey, A.G. McEwan, P.V. Bernhardt, A mechanistic and electrochemical study of the interaction between dimethyl sulfide dehydrogenase and its electron transfer partner cytochrome c2, J. Biol. Inorg. Chem. 13 (2008) 1231-1238.
460. R.A. Rothery, C.A. Trieber, J.H. Weiner, Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase, J. Biol. Chem. 274 (1999) 13002-13009.
461. C. Hagel, Struktur und Funktion der Ethylbenzol Dehydrogenase, einer anaeroben Kohlenwasserstoff-Hydroxylase (Dissertation), Technical University of Darmstadt, Darmstadt, 2006.
462. M.A. Picarra-Pereira, D.L. Turner, J. LeGall, A.V. Xavier, Structural studies on Desulfovibrio gigas cytochrome c3 by two-dimensional 1H-nuclear-magneticresonance spectroscopy, Biochem. J. 294 (Pt 3) (1993) 909-915. (Pubitemid 23286585)
463. R.K. Thauer, K. Jungermann, K. Decker, Energy conservation in anaerobic chemotrophic bacteria, Bacteriol. Rev. 41 (1977) 80.
464. A. Kröger, G. Unden, The function of menaquinone in bacterial electron transport, in: G. Lenaz (Ed.), Coenzyme Q: Biochemistry, Bioenergetics, and Clinical Applications of Ubiquinone, John Wiley and Sons Ltd., Chichester Wes Sussex; New York, 1985, pp. 285-300.
465. P. Infossi, E. Lojou, J.-P. Chauvin, G. Herbette, M. Brugna, M.-T. Giudici-Orticoni, Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: role of lipids and physiological partners in enzyme stability and activity, Int. J. Hydrog. Energy 35 (2010) 10778-10789.
466. R.K. Thauer, K. Jungermann, K. Decker, Energy conservation in chemotrophic anaerobic bacteria, Bacteriol. Rev. 41 (1977) 100-180. (Pubitemid 8082287)
467. F. Kapralek, The physiological role of tetrathionate respiration in growing citrobacter, J. Gen. Microbiol. 71 (1972) 133-139.
468. B.W. Vink, Stability relations of antimony and arsenic compounds in the light of revised and extended Eh-pH diagrams, Chem. Geol. 130 (1996) 9.
469. F. Maixner, M. Wagner, S. Lucker, E. Pelletier, S. Schmitz-Esser, K. Hace, E. Spieck, R. Konrat, D. Le Paslier, H. Daims, Environmental genomics reveals a functional chlorite dismutase in the nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii', Environ. Microbiol. 10 (2008) 3043-3056.