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Last modified: 31 March 1999

Bibliography on structural studies of DMSO reductase family

  1. Anderson, G.L., Williams, J. and Hille, R. (1992) The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum­containing hydroxylase. J. Biol. Chem. 267, 23674-23682.
  2. Augier, V., Guigliarelli, B., Asso, M., Bertrand, P., Frixon, C., Giordano, G., Chippaux, M. and Blasco, F. (1993a) Site­directed mutagenesis of conserved cysteine residues within the ß subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes. Biochemistry 32, 2013-2023.
  3. Augier, V., Asso, M., Guigliarelli, B., More, C., Bertrand, P., Santini, C.L., Blasco, F., Chippaux, M. and Giordano, G. (1993b) Removal of the high­potential [4Fe-4S] center of the ß­subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site­directed mutated enzymes. Biochemistry 32, 5099-5108.
  4. Barber, M.J., Siegel, L.M., Schauer, N.L., May, H.D. and Ferry, J.G. (1983) Formate dehydrogenase from Methanobacterium formicicum. Electron paramagnetic resonance spectroscopy of the molybdenum and iron-sulfur centers. J. Biol. Chem. 258, 10839-10845.
  5. Bastian, N.R., Kay, C.J., Barber, M.J. and Rajagopalan, K.V. (1991) Spectroscopic studies of the molybdenum­containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans. J. Biol. Chem. 266, 45-51.
  6. Bastian, N.R., Johnson, J.L. and Rajagopalan, K.V. (1992) 31P­NMR of free and protein­bound molybdopterin guanine dinucleotide. BioFactors 3, 197-200.
  7. Bastian, N.R., Foster, M.J. and Pope, J.C. (1995) Nitric oxide stabilizes the Mo(V) oxidation state of dimethyl sulfoxide reductase from Rhodobacter sphaeroides without inhibiting enzyme activity. BioFactors 5, 5-10.
  8. Baugh, P.E., Garner, C.D., Charnock, J.M., Collison, D., Davies, E.S., McAlpine, A.S., Bailey, S., Lane, I., Hanson, G.R. and McEwan, A.G. (1997) X­ray absorption spectroscopy of dimethylsulfoxide reductase from Rhodobacter capsulatus. J. Biol. Inorg. Chem. 2, 634-643.
  9. Bennett, B. and Bray, R.C. (1994) Redox­related activation and deactivation of E. coli nitrate reductase: kinetic and spectroscopic studies. Biochem. Soc. Trans. 22, 78S.
  10. Bennett, B., Benson, N., McEwan, A.G. and Bray, R.C. (1994a) Multiple states of the molybdenum centre of dimethylsulphoxide reductase from Rhodobacter capsulatus revealed by EPR spectroscopy. Eur. J. Biochem. 225, 321-331.
  11. Bennett, B., Benson, N., McEwan, A.G. and Bray, R.C. (1994b) E.p.r. characterisation of the molybdenum centre of Rhodobacter capsulatus dimethylsulphoxide reductase: New signals on reduction with Na2S2O4. Biochem. Soc. Trans. 22, 285S.
  12. Bennett, B., Berks, B.C., Ferguson, S.J., Thomson, A.J. and Richardson, D.J. (1994c) Mo(V) electron paramagnetic resonance signals from the periplasmic nitrate reductase of Thiosphaera pantotropha. Eur. J. Biochem. 226, 789-798.
  13. Bennett, B., Charnock, J.M., Sears, H.J., Berks, B.C., Thomson, A.J., Ferguson, S.J., Garner, C.D. and Richardson, D.J. (1996) Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X­ray absorption spectroscopy. Biochem. J. 317, 557-563.
  14. Benson, N., Farrar, J.A., McEwan, A.G. and Thomson, A.J. (1992) Detection of the optical bands of molybdenum(V) in DMSO reductase (Rhodobacter capsulatus) by low­temperature MCD spectroscopy. FEBS Lett. 307, 169-172.
  15. Berks, B.C., Richardson, D.J., Robinson, C., Reilly, A., Aplin, R.T. and Ferguson, S.J. (1994) Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha. Eur. J. Biochem. 220, 117-124.
  16. Berks, B.C., Richardson, D.J., Reilly, A., Willis, A.C. and Ferguson, S.J. (1995) The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha. Biochem. J. 309, 983-992.
  17. Bertram, P.A., Karrasch, M., Schmitz, R.A., Bocher, R., Albracht, S.P. and Thauer, R.K. (1994) Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. Eur. J. Biochem. 220, 477-484.
  18. Blum, H. and Poole, R.K. (1982) The molybdenum and iron-sulphur centres of Escherichia coli nitrate reductase are non­randomly oriented in the membrane. Biochem. Biophys. Res. Commun. 107, 903-909.
  19. Börner, G., Karrasch, M. and Thauer, R.K. (1991) Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg). FEBS Lett. 290, 31-34.
  20. Bosma, H.J., Wever, R. and van't Riet, J. (1978) Electron paramagnetic resonance studies on membrane­bound respiratory nitrate reductase of Klebsiella aerogenes. FEBS Lett. 90, 107-111.
  21. Boyington, J.C., Gladyshev, V.N., Khangulov, S.V., Stadtman, T.C. and Sun, P.D. (1997) Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275, 1305-1308.
  22. Bray, R.C., Vincent, S.P., Lowe, D.J., Clegg, R.A. and Garland, P.B. (1976) Electron­paramagnetic­resonance studies on the molybdenum of nitrate reductase from Escherichia coli K12. Biochem. J. 155, 201-203.
  23. Breton, J., Berks, B.C., Reilly, A., Thomson, A.J., Ferguson, S.J. and Richardson, D.J. (1994) Characterization of the paramagnetic iron­containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase. FEBS Lett. 345, 76-80.
  24. Cammack, R. and Weiner, J.H. (1990) Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli. Biochemistry 29, 8410-8416.
  25. Costa, C., Teixeira, M., LeGall, J., Moura, J.J.G. and Moura, I. (1997) Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774: Isolation and spectroscopic characterization of the active sites (heme, iron-sulfur centers and molybdenum). J. Biol. Inorg. Chem. 2, 198-208.
  26. Czjzek, M., Dos Santos, J.­P., Pommier, J., Giordano, G., Méjean, V. and Haser, R. (1998) Crystal structure of oxidized trimethylamine N­oxide reductase from Shewanella massilia at 2.5 Å resolution. J. Mol. Biol. 284, 435-447.
  27. Deaton, J.C., Solomon, E.I., Watt, G.D., Wetherbee, P.J. and Durfor, C.N. (1987) Electron paramagnetic resonance studies of the tungsten­containing formate dehydrogenase from Clostridium thermoaceticum. Biochem. Biophys. Res. Commun. 149, 424-430.
  28. Dias, J.M., Than, M.E., Humm, A., Huber, R., Bourenkov, G.P., Bartunik, H.D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., Moura, J.J.G., Moura, I. and Romão, M.J. (1999) Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods. Structure 7, 65-79.
  29. Durfor, C.N., Wetherbee, P.J., Deaton, J.C. and Solomon, E.I. (1983) Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum. Biochem. Biophys. Res. Commun. 115, 61-67.
  30. Forget, P. and DerVartanian, D.V. (1972) The bacterial nitrate reductases: EPR studies on nitrate reductase A from Micrococcus denitrificans. Biochim. Biophys. Acta 256, 600-606.
  31. Gadsby, P.M., Greenwood, C., Coddington, A., Thomson, A.J. and Godfrey, C. (1987) Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Electron­paramagnetic­resonance studies on the molybdenum centre. Biochem. J. 243, 235-239.
  32. Gangeswaran, R., Lowe, D.J. and Eady, R.R. (1993) Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii. Biochem. J. 289, 335-342.
  33. Garton, S.D., Hilton, J., Oku, H., Crouse, B.R., Rajagopalan, K.V. and Johnson, M.K. (1997) Active site structures and catalytic mechanism of Rhodobacter sphaeroides dimethyl sulfoxide reductase as revealed by resonance Raman spectroscopy. J. Am. Chem. Soc. 119, 12906-12916.
  34. George, G.N., Bray, R.C., Morpeth, F.F. and Boxer, D.H. (1985) Complexes with halide and other anions of the molybdenum centre of nitrate reductase from Escherichia coli. Biochem. J. 227, 925-931.
  35. George, G.N., Turner, N.A., Bray, R.C., Morpeth, F.F., Boxer, D.H. and Cramer, S.P. (1989) X­ray­absorption and electron­paramagnetic­resonance spectroscopic studies of the environment of molybdenum in high­pH and low­pH forms of Escherichia coli nitrate reductase. Biochem. J. 259, 693-700.
  36. George, G.N., Colangelo, C.M., Dong, J., Scott, R.A., Khangulov, S.V., Gladyshev, V.N. and Stadtman, T.C. (1998) X­ray absorption spectroscopy of the molybdenum site of Escherichia coli formate dehydrogenase. J. Am. Chem. Soc. 120, 1267-1273.
  37. George, G.N., Hilton, J., Temple, C., Prince, R.C. and Rajagopalan, K.V. (1999a) Structure of the molybdenum site of dimethyl sulfoxide reductase. J. Am. Chem. Soc. 121, 1256-1266.
  38. George, G.N., Costa, C., Moura, J.J.G. and Moura, I. (1999b) Observation of ligand­based redox chemistry at the active site of a molybdenum enzyme. J. Am. Chem. Soc. 121, 2625-2626.
  39. Gladyshev, V.N., Khangulov, S.V., Axley, M.J. and Stadtman, T.C. (1994) Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli. Proc. Natl. Acad. Sci. USA 91, 7708-7711.
  40. Gladyshev, V.N., Boyington, J.C., Khangulov, S.V., Grahame, D.A., Stadtman, T.C. and Sun, P.D. (1996) Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis. J. Biol. Chem. 271, 8095-8100.
  41. Godfrey, C., Greenwood, C., Thomson, A.J., Bray, R.C. and George, G.N. (1984) Electron­paramagnetic­resonance spectroscopy studies on the dissimilatory nitrate reductase from Pseudomonas aeruginosa. Biochem. J. 224, 601-608.
  42. Godfrey, C., Coddington, A., Greenwood, C., Thomson, A.J. and Gadsby, P.M. (1987a) Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Characterization of haem and iron-sulphur centres by magnetic­circular­dichroism and electron­paramagnetic­resonance spectroscopy. Biochem. J. 243, 225-233.
  43. Godfrey, C., Gadsby, P.M., Thomson, A.J., Greenwood, C. and Coddington, A. (1987b) Electron­paramagnetic­resonance and magnetic­circular­dichroism studies on the formate dehydrogenase-nitrate reductase particle from Pseudomonas aeruginosa. Biochem. J. 243, 241-248.
  44. Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G. and Bertrand, P. (1992) EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high­potential and a low­potential class and their relevance in the electron­transfer mechanism. Eur. J. Biochem. 207, 61-68.
  45. Guigliarelli, B., Magalon, A., Asso, M., Bertrand, P., Frixon, C., Giordano, G. and Blasco, F. (1996) Complete coordination of the four Fe-S centers of the ß 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, 4828-4836.
  46. Hewitt, E.J., Notton, B.A. and Garner, C.D. (1979) Nitrate reductases: properties and possible mechanism. Biochem. Soc. Trans. 7, 629-633.
  47. Hilton, J.C. and Rajagopalan, K.V. (1996) Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum. Arch. Biochem. Biophys. 325, 139-143.
  48. Johnson, J.L., Bastian, N.R., Schauer, N.L., Ferry, J.G. and Rajagopalan, K.V. (1991) Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum. FEMS Microbiol. Lett. 61, 213-216.
  49. Johnson, M.K., Bennett, D.E., Morningstar, J.E., Adams, M.W. and Mortenson, L.E. (1985) The iron-sulfur cluster composition of Escherichia coli nitrate reductase. J. Biol. Chem. 260, 5456-5463.
  50. Karrasch, M., Börner, G. and Thauer, R.K. (1990) The molybdenum cofactor of formylmethanofuran dehydrogenase from Methanosarcina barkeri is a molybdopterin guanine dinucleotide. FEBS Lett. 274, 48-52.
  51. Khangulov, S.V., Gladyshev, V.N., Dismukes, G.C. and Stadtman, T.C. (1998) Selenium­containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Biochemistry 37, 3518-3528.
  52. Kilpatrick, L., Rajagopalan, K.V., Hilton, J., Bastian, N.R., Stiefel, E.I., Pilato, R.S. and Spiro, T.G. (1995) Resonance Raman spectroscopic characterization of the molybdopterin active site of DMSO reductase. Biochemistry 34, 3032-3039.
  53. Knäblein, J., Dobbek, H., Ehlert, S. and Schneider, F. (1997) Isolation, cloning, sequence analysis and X­ray structure of dimethyl sulfoxide/trimethylamine N­oxide reductase from Rhodobacter capsulatus. Biol. Chem. 378, 293-302.
  54. McAlpine, A.S., McEwan, A.G., Shaw, A.L. and Bailey, S. (1997) Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: Crystal structure of the oxidised enzyme at 1.82­Å resolution and the dithionite­reduced enzyme at 2.8­Å resolution. J. Biol. Inorg. Chem. 2, 690-701.
  55. McAlpine, A.S., McEwan, A.G. and Bailey, S. (1998) The high resolution crystal structure of DMSO reductase in complex with DMSO. J. Mol. Biol. 275, 613-623.
  56. Magalon, A., Rothery, R.A., Giordano, G., Blasco, F. and Weiner, J.H. (1997) Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate. J. Bacteriol. 179, 5037-5045.
  57. Magalon, A., Lemesle­Meunier, D., Rothery, R.A., Frixon, C., Weiner, J.H. and Blasco, F. (1997) Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A. J. Biol. Chem. 272, 25652-25658.
  58. Magalon, A., Asso, M., Guigliarelli, B., Rothery, R.A., Bertrand, P., Giordano, G. and Blasco, F. (1998) Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: Investigation by site­directed mutagenesis of the conserved His­50 residue in the NarG subunit. Biochemistry 37, 7363-7370.
  59. May, H.D., Schauer, N.L. and Ferry, J.G. (1986) Molybdopterin cofactor from Methanobacterium formicicum formate dehydrogenase. J. Bacteriol. 166, 500-504.
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  62. Rothery, R.A. and Weiner, J.H. (1993) Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster. Biochemistry 32, 5855-5861.
  63. Rothery, R.A. and Weiner, J.H. (1996) Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase. Biochemistry 35, 3247-3257.
  64. Rothery, R.A., Grant, J.L., Johnson, J.L., Rajagopalan, K.V. and Weiner, J.H. (1995) Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation. J. Bacteriol. 177, 2057-2063.
  65. Schneider, F., Löwe, J., Huber, R., Schindelin, H., Kisker, C. and Knäblein, J. (1996) Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution. J. Mol. Biol. 263, 53-69.
  66. Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K.V. and Rees, D.C. (1996) Crystal structure of DMSO reductase: Redox­linked changes in molybdopterin coordination. Science 272, 1615-1621.
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  69. Sears, H.J., Bennett, B., Spiro, S., Thomson, A.J. and Richardson, D.J. (1995) Identification of periplasmic nitrate reductase Mo(V) EPR signals in intact cells of Paracoccus denitrificans. Biochem. J. 310, 311-314.
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  71. Solomon, P.S., Lane, I., Hanson, G.R. and McEwan, A.G. (1997) Characterisation of the pterin molybdenum cofactor in dimethylsulfoxide reductase of Rhodobacter capsulatus. Eur. J. Biochem. 246, 200-203.
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  75. van't Riet, J., van Ed, J.H., Wever, R., van Gelder, B.F. and Planta, R.J. (1975) Characterization of the respiratory nitrate reductase of Klebsiella aerogenes as a molybdenum­containing iron-sulfur enzyme. Biochim. Biophys. Acta 405, 306-317.
  76. Vincent, S.P. and Bray, R.C. (1978) Electron­paramagnetic­resonance studies on nitrate reductase from Escherichia coli K12. Biochem. J. 171, 639-647.
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