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Last modified: 10 December 1998

Bibliography on structural studies of haemerythrin­like proteins

  1. Clarke, S.E., Sieker, L.C., Stenkamp, R.E. and Sanders­Loehr, J. (1979) Mercury binding to hemerythrin. Coordination of mercury and its effects on subunit interactions. Biochemistry 18, 684-689.
  2. DeRose, V.J., Liu, K.E., Kurtz, D.M., Jr., Hoffman, B.M. and Lippard, S.J. (1993) Protein ENDOR identification of bridging hydroxide ligands in mixed­valent diiron centers of proteins: methane monooxygenase and semimet azidohemerythrin. J. Am. Chem. Soc. 115, 6440-6441.
  3. Dikanov, S.A., Davydov, R.M., Gräslund, A., and Bowman. M.K. (1998) Two­dimensional ESEEM spectroscopy of nitrogen hyperfine couplings in methemerythrin and azidomethemerythrin. J. Am. Chem. Soc. 120, 6797-6805.
  4. Dunn, J.B., Shriver, D.F. and Klotz, I.M. (1975) Resonance Raman studies of hemerythrin-ligand complexes. Biochemistry 14, 2689-2695.
  5. Dunn, J.B., Addison, A.W., Bruce, R.E., Sanders­Loehr, J. and Loehr, T.M. (1977) Comparison of hemerythrins from four species of sipunculids by optical absorption, circular dichroism, fluorescence emission, and resonance Raman spectroscopy. Biochemistry 16, 1743-1749.
  6. Freier, S.M., Duff, L.L., van Duyne, R.P. and Klotz, I.M. (1979) Resonance Raman studies and structure of a sulfide complex of methemerythrin. Biochemistry 18, 5372-5377.
  7. Freier, S.M., Duff, L.L., Shriver, D.F. and Klotz, I.M. (1980) Resonance Raman spectroscopy of iron­oxygen vibrations in hemerythrin. Arch. Biochem. Biophys. 205, 449-463.
  8. Garbett, K., Darnall, D.W., Klotz, I.M. and Williams, R.J.P. (1969) Spectroscopy and structure of hemerythrin. Arch. Biochem. Biophys. 135, 419-434.
  9. Harrington, P.C., Muhoberac, B.B., Wharton, D.C. and Wilkins, R.G. (1981) Some redox properties of myohemerythrin from retractor muscle of Themiste zostericola. Biochemistry 20, 6134-6139.
  10. Hendrickson, W.A. and Klippenstein, G.L. (1974) Crystals of myohemerythrin. J. Mol. Biol. 87, 147-149.
  11. Hendrickson, W.A. and Ward, K.B. (1977) Pseudosymmetry in the structure of myohemerythrin. J. Biol. Chem. 252, 3012-3018.
  12. Hendrickson, W.A., Klippenstein, G.L. and Ward, K.B. (1975) Tertiary structure of myohemerythrin at low resolution. Proc. Natl. Acad. Sci. USA 72, 2160-2164.
  13. Hendrickson, W.A., Co, M.S., Smith, J.L., Hodgson, K.O. and Klippenstein, G.L. (1982) X­ray absorption spectroscopy of the dimeric iron site in azidomethemerythrin from Phascolopsis gouldii. Proc. Natl. Acad. Sci. USA 79, 6255-6259.
  14. Hoffman, B.M., Sturgeon, B.E., Doan, P.E., DeRose, V.J., Liu, K.E. and Lippard, S.J. (1994) ESEEM and ENDOR magnetic resonance studies of the non­Kramers doublet in the integer­spin diiron(II)forms of two methane monooxygenase hydroxylases and hemerythrin azide. J. Am. Chem. Soc. 116, 6023-6024.
  15. Holmes, M.A. and Stenkamp, R.E. (1991) Structures of met and azidomet hemerythrin at 1.66 Å resolution. J. Mol. Biol. 220, 723-737.
  16. Holmes, M.A., Le Trong, I., Turley, S., Sieker, L.C. and Stenkamp, R.E. (1991) Structures of deoxy and oxy hemerythrin at 2.0 Å resolution. J. Mol. Biol. 218, 583-593.
  17. Kaminaka, S., Takizawa, H., Handa, T., Kihara, H. and Kitagawa, T. (1992) Resonance Raman study on the active­site structure of a cooperative hemerythrin. Biochemistry 31, 6997-7002.
  18. Kurtz, D.M., Jr., Sage, J.T., Hendrich, M., Debrunner, P.G. and Lukat, G.S. (1983) Semi­met oxidation level of chalcogenide derivatives of methemerythrin. Mössbauer and EPR studies. J. Biol. Chem. 258, 2115-2117.
  19. Langerman, N. and Sturtevant, J.M. (1971) Calorimetric studies of quaternary structure and ligand­binding hemerythrin. Biochemistry 10, 2809-2815.
  20. Lukat, G.S., Kurtz, D.M., Jr., Shiemke, A.K. Loehr, T.M. and Sanders­Loehr, J. (1984) Sulfide­bridged derivatives of the binuclear iron site of hemerythrin at both met and semi­met oxidation levels. Biochemistry 23, 6416-6422.
  21. McCallum, J.D., Shiemke, A.K. and Sanders­Loehr, J. (1984) Hydroxide ion binding to methemerythrin. An investigation by resonance Raman and difference spectroscopy. Biochemistry 23, 2819-2825.
  22. Martins, L.J., Hill, C.P. and Ellis, W.R., Jr. (1997) Structures of wild­type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 Å resolution. Biochemistry 36, 7044-7049.
  23. Muhoberac, B.B., Wharton, D.C., Babcock, L.M., Harrinton, P.C. and Wilkins, R.G. (1980) EPR spectroscopy of semi­methemerythrin. Biochim. Biophys. Acta 626, 337-345.
  24. Nocek, J.M., Kurtz, D.M., Jr., Pickering, R.A. and Doyle, M.P. (1984) Oxidation of deoxyhemerythrin to semi­methemerythrin by nitrite. J. Biol. Chem. 259, 12334-12338.
  25. Nocek, J.M., Kurtz, D.M., Jr., Sage, J.T., Xia, Y.M., Debrunner, P.G., Shiemke, A.K., Sanders­Loehr, J. and Loehr, T.M. (1988) Nitric oxide adducts of the binuclear iron site of hemerythrin: spectroscopy and reactivity. Biochemistry 27, 1014-1024.
  26. Pulver, S.C., Froland, W.A., Fox, B.G., Lipscomb, J.D. and Solomon, E.I. (1993) Spectroscopic studies of the coupled binuclear non­heme iron active site in the fully reduced hydroxylase component of methane monooxygenase: Comparison to deoxy and deoxy­azide hemerythrin. J. Am. Chem. Soc. 115, 12409-12422.
  27. Raner, G.M., Martins, L.J. and Ellis, W.R., Jr. (1997) Functional role of leucine­103 in myohemerythrin. Biochemistry 36, 7037-7043.
  28. Reymond, M.T., Huo, S., Duggan, B., Wright, P.E. and Dyson, H.J. (1997) Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31­residue peptide from the C terminus of myohemerythrin. Biochemistry 36, 5234-5244.
  29. Richardson, D.E., Emad, M., Reem, R.C. and Solomon, E.I. (1987) Allosteric interactions in sipunculid and brachiopod hemerythrins. Biochemistry 26, 1003-1013.
  30. Sheriff, S., Hendrickson, W.A., Stenkamp, R.E., Sieker, L.C. and Jensen, L.H. (1985) Influence of solvent accessibility and intermolecular contacts on atomic mobilities in hemerythrins. Proc. Natl. Acad. Sci. USA 82, 1104-1107.
  31. Sheriff, S., Hendrickson, W.A. and Smith, J.L. (1987) Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197, 273-296.
  32. Smith, J.L., Hendrickson, W.A. and Addison, A.W. (1983) Structure of trimeric haemerythrin. Nature 303, 86-88.
  33. Stemmler, T.L., Sossong, T.M., Jr., Goldstein, J.I., Ash, D.E., Elgren, T.E., Kurtz, D.M., Jr., and Penner­Hahn, J.E. (1997) EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganese­substituted ribonucleotide reductase and hemerythrin. Biochemistry 36, 9847-9858.
  34. Stenkamp, R.E., Sieker, L.C. and Jensen, L.H. (1976a) Structure of the iron complex in methemerythrin. Proc. Natl. Acad. Sci. USA 73, 349-351.
  35. Stenkamp, R.E., Sieker, L.C., Jensen, L.H. and Sanders­Loehr, J. (1976b) Structure of methemerythrin at 5 Å resolution. J. Mol. Biol. 100, 23-34.
  36. Stenkamp, R.E., Sieker, L.C., Jensen, L.H. and McQueen, J.E. (1978) Structure of methemerythrin at 2.8­Å resolution: computer graphics fit of an averaged electron density map. Biochemistry 17, 2499-2504.
  37. Stenkamp, R.E., Sieker, L.C., Jensen, L.H., McCallum, J.D. and Sanders­Loehr, J. (1985) Active site structures of deoxyhemerythrin and oxyhemerythrin. Proc. Natl. Acad. Sci. USA 82, 713-716.
  38. Sturgeon, B.E., Doan, P.E., Liu, K.E., Burdi, D., Tong, W.H., Nocek, J.M., Gupta, N., Stubbe, J., Kurtz, Jr., D.M., Lippard, S.J. and Hoffman, B.M. (1997) Non­Kramers ESEEM of integer­spin diferrous carboxylate­bridged clusters in proteins. J. Am. Chem. Soc. 119, 375-386.
  39. Thomann, H., Bernardo, M., McCormick, J.M., Pulver, S.C., Andersson, K.K., Lipscomb, J.D. and Solomon, E.I. (1993) Pulsed EPR studies of mixed valent [Fe(II)Fe(III)] forms of hemerythrin and methane monooxygenase: Evidence for a hydroxide bridge. J. Am. Chem. Soc. 115, 8881-8882.
  40. Utecht, R.E. and Kurtz, D.M., Jr. (1988) Cytochrome b5 and NADH-cytochrome­b5 reductase from sipunculan erythrocytes. A methemerythrin reduction system from Phascolopsis gouldii. Biochim. Biophys. Acta 953, 164-178.
  41. Wang, Z., Martins, L., Ellis, W.R., Jr. and Que, L., Jr. (1997) Proton NMR studies of myohemerythrin from Themiste zostericola. J. Biol. Inorg. Chem. 2, 56-64.
  42. Ward, K.B., Hendrickson, W.A. and Klippenstein, G.L. (1975) Quaternary and tertiary structure of haemerythrin. Nature 257, 818-821.
  43. York, J.L., Millett, F.S. and Minor, L.B. (1980) Proton magnetic resonance study of the histidines in hemerythrin and chemical identification of the nonligand histidines. Biochemistry 19, 2583-2588.
  44. Zhang, J.­H. and Kurtz, D.M., Jr. (1992) Metal substitutions at the diiron sites of hemerythrin and myohemerythrin: contributions of divalent metals to stability of a four­helix bundle protein. Proc. Natl. Acad. Sci. USA 89, 7065-7069.
  45. Zhang, J.­H., Kurtz, D.M., Jr., Xia, Y.­M. and Debrunner, P.G. (1992) Conversion of non­functional to functional iron following reconstitution of hemerythrin. Biochim. Biophys. Acta 1122, 293-298.
  46. Zhang, K., Stern, E.A., Ellis, F., Sanders­Loehr, J. and Shiemke, A.K. (1988) The active site of hemerythrin as determined by X­ray absorption fine structure. Biochemistry 27, 7470-7479.
Reviews on haemerythrin family proteins