TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 14 October 1996
Last modified: 13 August 1998

Bibliography on structural studies of sirohaem-Fe4S4 enzymes

  1. Aparicio, P.J., Knaff, D.B. and Malkin, R. (1975) The role of an iron-sulfur center and siroheme in spinach nitrite reductase. Arch. Biochem. Biophys. 169, 102-107.
  2. Arendsen, A.F., Verhagen, M.F.J.M., Wolbert, R.B.G., Pierik, A.J., Stams, A.J.M., Jetten, M.S.M. and Hagen, W.R. (1993) The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S=9/2 iron-sulfur clusters. Biochemistry 32, 10323-10330.
  3. Belinsky, M.I. (1996) Hyperfine evidence of strong double exchange in multimetallic {[Fe4S4]-Fe} active center of Escherichia coli sulfite reductase. J. Biol. Inorg. Chem. 1, 186-188.
  4. Christner, J.A., Münck, E., Janick, P.A. and Siegel, L.M. (1981) Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups. J. Biol. Chem. 256, 2098-2101.
  5. Christner, J.A., Münck, E., Janick, P.A. and Siegel, L.M. (1983a) Mössbauer evidence for exchange­coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase. Studies of the reduced states and of a nitrite turnover complex. J. Biol. Chem. 258, 11147-11156.
  6. Christner, J.A., Janick, P.A., Siegel, L.M. and Münck, E. (1983b) Mössbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster. J. Biol. Chem. 258, 11157-11164.
  7. Cline, J.F., Janick, P.A., Siegel, L.M. and Hoffman, B.M. (1985) Electron­nuclear double resonance studies of oxidized Escherichia coli sulfite reductase: 1H, 14N, and 57Fe measurements. Biochemistry 24, 7942-7947.
  8. Cline, J.F., Janick, P.A., Siegel, L.M. and Hoffman, B.M. (1986) 57Fe and 1H electron­nuclear double resonance of three doubly reduced states Escherichia coli sulfite reductase. Biochemistry 25, 4647-4654.
  9. Crane, B.R., Siegel, L.M. and Getzoff, E.D. (1995) Sulfite reductase structure at 1.6 Å: Evolution and catalysis for reduction of inorganic anions. Science 270, 59-67.
  10. Crane, B.R., Bellamy, H. and Getzoff, E.D. (1997a) Multiwavelength anomalous diffraction of sulfite reductase hemoprotein: Making the most of MAD data. Acta Crystallogr. D53, 8-22.
  11. Crane, B.R., Siegel, L.M. and Getzoff, E.D. (1997b) Structures of the siroheme­ and Fe4S4­containing active center of sulfite reductase in different states of oxidation: Heme activation via reduction­gated exogenous ligand exchange. Biochemistry 36, 12101-12119.
  12. Crane, B.R., Siegel, L.M. and Getzoff, E.D. (1997c) Probing the catalytic mechanism of sulfite reductase by X­ray crystallography: Structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products. Biochemistry 36, 12120-12137.
  13. Day, E.P., Peterson, J., Bonvoisin, J.J., Young, L.J., Wilkerson, J.O. and Siegel, L.M. (1988) Magnetization of the sulfite and nitrite complexes of oxidized sulfite and nitrite reductases: EPR silent spin S=½ states. Biochemistry 27, 2126-2132.
  14. DerVartanian, D.V. (1994) Desulforubidin: dissimilatory, high­spin sulfite reductase of Desulfomicrobium species. Methods Enzymol. 243, 270-276.
  15. Fauque, G., Lino, A.R., Czechowski, M., Kang, L., DerVartanian, D.V.G., Moura, J.J.G., LeGall, J. and Moura, I. (1990) Purification and characterization of bisulfite reductase (desulfofuscidin) from Desulfovibrio thermophilus and its complexes with exogenous ligands. Biochim. Biophys. Acta 1040, 112-118.
  16. Han, S.H., Madden, J.F., Thompson, R.G., Strauss, S.H., Siegel, L.M. and Spiro, T.G. (1989a) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry 28, 5461-5471.
  17. Hall, M.H., Prince, R.H. and Cammack, R. (1979) EPR spectroscopy of the iron-sulphur cluster and sirohaem in the dissimilatory sulphite reductase (desulphoviridin) from Desulphovibrio gigas. Biochim. Biophys. Acta 581, 27-33.
  18. Han, S.H., Madden, J.F., Siegel, L.M. and Spiro, T.G. (1989b) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. Biochemistry 28, 5477-5485.
  19. Hatchikian, E.C. (1994) Desulfofuscidin: dissimilatory, high­spin sulfite reductase of thermophilic, sulfate­reducing bacteria. Methods Enzymol. 243, 276-295.
  20. Hirasawa­Soga, M., Tamura, G. and Horie, S. (1983) Spectrophotometric and electron spin resonance studies on the substrate interactions of ferredoxin­linked nitrite reductase from spinach. J. Biochem. (Tokyo) 94, 1833-1840.
  21. Huynh, B.­H., Kang, L., DerVartanian, D.V., Peck, H.D., Jr. and LeGall, J. (1984) Characterization of a sulfite reductase from Desulfovibrio vulgaris. Evidence for the presence of a low­spin siroheme and an exchange­coupled siroheme­[4Fe-4S] unit. J. Biol. Chem. 259, 15373-15376.
  22. Janick, P.A. and Siegel, L.M. (1982) Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and Fe4S4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit. Biochemistry 21, 3538-3547.
  23. Janick, P.A. and Siegel, L.M. (1983) Electron paramagnetic resonance and optical evidence for interaction between siroheme and Fe4S4 prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands. Biochemistry 22, 504-515.
  24. Janick, P.A., Rueger, D.C., Krueger, R.J., Barber, M.J. and Siegel, L.M. (1983) Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite. Biochemistry 22, 396-408.
  25. Kang, L., LeGall, J., Kowal, A.T. and Johnson, M.K. (1987) Spectroscopic properties of siroheme extracted from sulfite reductases. J. Inorg. Biochem. 30, 273-290.
  26. Kaufman, J., Spicer, L.D. and Siegel, L.M. (1993a) Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit. Biochemistry 32, 2853-2867.
  27. Kaufman, J., Siegel, L.M. and Spicer, L.D. (1993b) Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands. Biochemistry 32, 8782-8791.
  28. Krueger, R.J. and Siegel, L.M. (1982a) Spinach siroheme enzymes: Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase. Biochemistry 21, 2892-2904.
  29. Krueger, R.J. and Siegel, L.M. (1982b) Evidence for siroheme-Fe4S4 interaction in spinach ferredoxin-sulfite reductase. Biochemistry 21, 2905-2909.
  30. Lui, S.M., Soriano, A. and Cowan, J.A. (1994) Electronic properties of the dissimilatory sulphite reductase from Desulfovibrio vulgaris (Hildenborough): comparative studies of optical spectra and relative reduction potentials for the [Fe4S4]-sirohaem prosthetic centres. Biochem. J. 304, 441-447.
  31. McRee, D.E., Richardson, D.C., Richardson, J.S. and Siegel, L.M. (1986) The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase. J. Biol. Chem. 261, 10277-10281.
  32. Madden, J.F., Han, S.H., Siegel, L.M. and Spiro, T.G. (1989) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. Biochemistry 28, 5471-5477.
  33. Matthews, J.C., Timkovich, R., Liu, M.Y. and LeGall, J. (1995) Siroamide: a prosthetic group isolated from sulfite reductases in the genus Desulfovibrio. Biochemistry 34, 5248-5251.
  34. Moura, I., Lino, A.R., Moura, J.J.G., Xavier, A.V., Fauque, G., Peck, H.D., Jr. and LeGall, J. (1986) Low­spin sulfite reductases: a new homologous group of non­heme iron­siroheme proteins in anaerobic bacteria. Biochem. Biophys. Res. Commun. 141, 1032-1041.
  35. Münck, E. (1982) Mössbauer studies of [3Fe­3S] clusters and sulfite reductase. In Spiro, T.G., Ed. Iron-sulfur proteins. Wiley, New York, pp. 147-175.
  36. Ostrowski, J., Wu, J.­Y., Rueger, D.C., Miller, B.E., Siegel, L.M. and Kredich, N.M. (1989) Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme­Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase. J. Biol. Chem. 264, 15726-15737.
  37. Pierik, A.J. and Hagen, W.R. (1991) S=9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. Eur. J. Biochem. 195, 505-516.
  38. Seki, Y., Nagai, Y. and Ishimoto, M. (1985) Characterization of a dissimilatory&$173;type sulfite reductase, desulfoviridin, from Desulfovibrio africanus Benghazi. J. Biochem. (Tokyo) 98, 1535-1543.
  39. Siegel, L.M., Rueger, D.C., Barber, M.J., Krueger, R.J., Orme­Johnson, N.R. and Orme­Johnson, W.H. (1982) Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes. J. Biol. Chem. 257, 6343-6350.
  40. Steuber, J., Arendsen, A.F., Hagen, W.R. and Kroneck, P.M. (1995) Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex) and comparison with the enzyme from Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 233, 873-879.
  41. Underwood­Lemons, T., Moura, I. and Yue, K.T. (1993) Resonance Raman study of sirohydrochlorin and siroheme in sulfite reductases from sulfate reducing bacteria. Biochim. Biophys. Acta 1157, 275-284.
  42. Wolfe, B.M., Lui, S.M. and Cowan, J.A. (1994) Desulfoviridin, a multimeric­dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies. Eur. J. Biochem. 223, 79-89.
  43. Young, L.J. and Siegel, L.M. (1988a) Activated conformers of Escherichia coli sulfite reductase heme protein subunit. Biochemistry 27, 4991-4999.
  44. Young, L.J. and Siegel, L.M. (1988b) Superoxidized states of Escherichia coli sulfite reductase heme protein subunit. Biochemistry 27, 5984-5990.