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General references on structure and function of haem proteins

Reviews and original papers

  1. Aida, T. and Inoue, S. (1998) Metalloporphyrins as initiators for living and immortal polymerizations. Acc. Chem. Res. 29, 39-48.
  2. Andersson, L.A. and Dawson, L.A. (1991) EXAFS spectroscopy of heme­containing oxygenases and peroxidases. Structure and Bonding 64, 1-40.
  3. Armstrong, F.A. (1990) Probing metalloproteins by voltammetry. Structure and Bonding 72, 137-221.
  4. Armstrong, W.H. (1988) Metalloprotein crystallography: Survey of recent results and relationships to model studies. In Que, L., Jr., Ed. ACS Symposium Series 372: Metal Clusters in Proteins. American Chemical Society, Washington, pp. 1-27.
  5. Austin, J.C., Rodgers, K.R. and Spiro, T.G. (1993) Protein structure from ultraviolet resonance Raman spectroscopy. Methods Enzymol. 226, 374-396.
  6. Averill, B.A. (1996) Dissimilatory nitrite and nitric oxide reductases. Chem. Rev. 96, 2951-2964.
  7. Barrick, D. (1995) Depletion and replacement of protein metal ligands. Curr. Opin. Biotechnol. 6, 411-418.
  8. Bearden, A.J. and Dunham, W.R. (1970) Iron electronic configuration in proteins: Studies by Mössbauer spectroscopy. Structure and Bonding 8, 1-52.
  9. Brittain, T., Greenwood, C., Springall, J.P. and Thomson, A.J. (1978) Magnetic­circular­dichroism studies of haem a and its derivatives. Biochem. J. 173, 411-417.
  10. Bonnett, R. (1981) Oxygen activation and tetrapyrroles. Essays Biochem. 17, 1-51.
  11. Chang, C.K. (1994) Haem d1 and other haem cofactors from bacteria. Ciba Found. Symp. 180, 228-238.
  12. Chapman, S.K., Daff, S. amd Munro, A.W. (1997) Heme: the most versatile redox centre in biology? Structure and Bonding 88, 39-70.
  13. Cohen, I.A. (1980) Metal-metal interactions in metalloporphyrins, metalloproteins and metalloenzymes. Structure and Bonding 40, 1-37.
  14. Cole, S.P. and Marks, G.S. (1984) Ferrochelatase and N­alkylated porphyrins. Mol. Cell. Biochem. 64, 127-137.
  15. Cupane, A., Leone, M., Vitrano, E. and Cordone, L. (1995) Low temperature optical absorption spectroscopy: An approach to the study of stereodynamic properties of hemeproteins. Eur. Biophys. J. 23, 385-398.
  16. Dailey, H.A. (1997) Enzymes of heme biosynthesis. J. Biol. Inorg. Chem. 2, 411-417.
  17. Dawson, J.H. (1988) Probing structure­function relations in heme­containing oxygenases and peroxidases. Science 240, 433-439.
  18. Degli Esposti, M. (1989) Prediction and comparison of the haem­binding sites in membrane haemoproteins. Biochim. Biophys. Acta 977, 249-265.
  19. Dreyer, J.L. (1984) Electron transfer in biological systems: an overview. Experientia 40, 653-675.
  20. Dunn, R.C., Xie, X.L. and Simon, J.D. (1993) Real­time spectroscopic techniques for probing conformational dynamics of heme proteins. Methods Enzymol. 226, 177-198.
  21. Duval, H., Bulach, V., Fischer, J., Renner, M.W., Fajer, J. and Weiss, R. (1997) Correlation of macrocycle distortion with oxidation potentials of iron(III) porphyrins: Molecule structure of the sterically crowded chloro­iron(III) 7,8,17,18­tetrabromo­5,10,15,20­tetraphenylporphyrin. J. Biol. Inorg. Chem. 2, 662-666. [Electronic Supplementary Material]
  22. Ehrenberg, A. (1965) The biochemistry of heme­iron. Z. Naturwiss. Med. Grundlagenforsch. 2, 203-219.
  23. Falk, J.E. (1967) Bond structure in haem compounds. Enzymologia 32, 3-12.
  24. Frieden, E. (1974) The evolution of metals as essential elements (with special reference to iron and copper). Adv. Exp. Med. Biol. 48, 1-29.
  25. Fuhrhop, J.­H. (1974) The oxidation states and reversible redox reactions of metalloporphyrins. Structure and Bonding 18, 1-67.
  26. Fuhrhop, J.­H. (1976) Molecular complexes and oxygen adducts of tetrapyrrole pigments. Angew. Chem. Int. Ed. Engl. 15, 648-659.
  27. Gersonde, K. (1972) Interaction between heme group and protein structure. Hämatol. Bluttransfus. 10, 183-190.
  28. Gibney, B.R., Rabanal, F., Reddy, K.S. and Dutton, P.L. (1998) Effect of four helix bundle topology on heme binding and redox properties. Biochemistry 37, 4635-4643.
  29. Ghosh, A. (1998) First­principles quantum chemical studies of porphyrins. Acc. Chem. Res. 31, 189-198.
  30. Ghosh, A. and Vangberg, T. (1998) Comparative thermochemistry of metalloporphyrin isomers as a function of metal ion size. A possible insight into Nature's choice of porphyrin over isomeric ligands. Inorg. Chem. 37, 6276-6280. Computation
  31. Ghosh, A., Gonzalez, E. and Vangberg, T. (1999) Theoretical studies of low­spin six­coordinate iron(III) porphyrins relevant to cytochromes b: Variable electronic configurations, ligand noninnocence, and macrocycle ruffling. J. Phys. Chem. B103, 1363-1367. Computation
  32. Goldman, B.S., Beck, D.L., Monika, E.M. and Kranz, R.G. (1998) Transmembrane heme delivery systems. Proc. Natl. Acad. Sci. USA 95, 5003-5008.
  33. Goto, Y. and Fink, A.L. (1994) Acid­induced folding of heme proteins. Methods Enzymol. 232, 3-15.
  34. Granick, S. and Beale, S.I. (1978) Hemes, chlorophylls, and related compounds: Biosynthesis and metabolic regulation. Adv. Enzymol. Relat. Areas Mol. Biol. 46, 33-203.
  35. Gross, Z. (1996) The effect of axial ligands on the reactivity and stability of the oxoferryl moiety in model complexes of Compound I of heme­dependent enzymes. J. Biol. Inorg. Chem. 1, 368-371.
  36. Gunner, M.R., Alexov, E., Torres, E. and Lipovaca, S. (1997) The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis. J. Biol. Inorg. Chem. 2, 126-134.
  37. Gunsalus, I.C., Sligar, S.G., Nordlund, T. and Frauenfelder, H. (1977) Oxygen sensing heme proteins: monoxygenases, myoglobin and hemoglobin. Adv. Exp. Med. Biol. 78, 37-50.
  38. Hendry, G.A. and Jones, O.T. (1980) Haems and chlorophylls: comparison of function and formation. J. Med. Genet. 17, 1-14.
  39. Henry, Y., Lepoivre, M., Drapier, J.­C., Ducrocq, C., Boucher, J.­L. and Guissani, A. (1993) EPR characterization of molecular targets for NO in mammalian cells and organelles. FASEB J. 7, 1124-1134.
  40. Hilinski, E.F. and Rentzepis, P.M. (1983) Biological applications of picosecond spectroscopy. Nature 302, 481-487.
  41. Hoffmann, B.M., Natan. M.J., Nocek, J.M. and Wallin, S.A. (1991) Long­range electron transfer within metal­substituted protein complexes. Structure and Bonding 75, 85-108.
  42. Jordan, P.M. (1995) Highlights in haem biosynthesis. Curr. Opin. Struct. Biol. 4, 902-911.
  43. Kalyanaraman, B. (1996) Detection of nitric oxide by electron spin resonance in chemical, photochemical, cellular, physiological, and pathophysiological systems. Methods Enzymol. 268, 168-187.
  44. Kitagawa, T. and Ozaki, Y. (1987) Infrared and Raman spectra of metalloporphyrins. Structure and Bonding 64, 71-114.
  45. Lang, G. (1970) Mössbauer spectroscopy of haem proteins. Q. Rev. Biophys. 3, 1-60.
  46. Le Gall, J., Payne, W.J., Chen, L., Liu, M.Y. and Xavier, A.V. (1994) Localization and specificity of cytochromes and other electron transfer proteins from sulfate­reducing bacteria. Biochimie 76, 655-665.
  47. Li, H. and Poulos, T.L. (1994) Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures. Structure 2, 461-464.
  48. Lowe, D.J. (1992) ENDOR and EPR of metalloproteins. Prog. Biophys. Mol. Biol. 57, 1-22.
  49. McMahon, M.T., deDios, A.C., Godbout, N., Salzmann, R., Laws, D.D., Le, H., Havlin, R.H. and Oldfield, E. (1998) An experimental and quantum chemical investigation of CO binding to heme proteins and model systems: A unified model based on 13C, 17O, and 57Fe nuclear magnetic resonance and 57Fe Mössbauer and infrared spectroscopies. J. Am. Chem. Soc. 120, 4784-4797.
  50. Marks, G.S. (1987) Interaction of chemicals with hemoproteins: implications for the mechanism of action of porphyrinogenic drugs and nitroglycerin. Can. J. Physiol. Pharmacol. 65, 1111-1119.
  51. Mauk, A.G. and Moore, G.R. (1997) Control of metalloprotein redox potentials: what does site­directed mutagenesis of hemoproteins tell us? J. Biol. Inorg. Chem. 2, 119-125.
  52. Mazumdar, S. and Mitra, S. (1993) Biomimetic chemistry of hemes inside aqueous micelles. Structure and Bonding 81, 115-145.
  53. Meyer, T.E. (1991) Evolution of cytochromes and photosynthesis. Biochim. Biophys. Acta 1058, 31-34.
  54. Miller, R.J. (1991) Vibrational energy relaxation and structural dynamics of heme proteins. Annu. Rev. Phys. Chem. 42, 581-614.
  55. Mogi, T., Saiki, K. and Anraku, Y. (1994) Biosynthesis and functional role of haem o and haem a. Mol. Microbiol. 14, 391-398.
  56. Momot, K.I. and Walker, F.A. (1998) 1H NMR studies of paramagnetic metalloporphyrin complexes: Rotation of axial ligands, proton relaxation, and NOE detectability. http://www.chem.arizona.edu/faculty/walk/NMREC3/.
  57. Moore, G.R. (1991) Bacterial 4­alpha­helical bundle cytochromes. Biochim. Biophys. Acta 1058, 38-41.
  58. Morgan, B. and Dolphin, D. (1987) Synthesis and structure of biomimetic porphyrins. Structure and Bonding 64, 115-203.
  59. Moser, C.C., Page, C.C., Farid, R. and Dutton, P.L. (1995) Biological electron transfer. J. Bioenerg. Biomembr. 27, 263-274.
  60. Nakamoto, K. and Czernuszewicz, R.S. (1993) Infrared spectroscopy. Methods Enzymol. 226, 259-289.
  61. Nakamura, M., Ikeue, T., Fujii, H., Yoshimura, T. and Tajima, K. (1998) Electron configuration and spin distribution in low­spin (meso­tetraalkylporphyrinato)iron(III) complexes carrying one or two orientationally fixed imidazole ligands. Inorg. Chem. 37, 2405-2414.
  62. Neilands, J.B. (1972) Evolution of biological iron binding centers. Structure and Bonding 11, 145-170.
  63. Nordmann, R., Ribiere, C. and Rouach, H. (1987) Involvement of iron and iron­catalyzed free radical production in ethanol metabolism and toxicity. Enzyme 37, 57-69.
  64. Onuchic, J.N., Beratan, D.N., Winkler, J.R. and Gray, H.B. (1992) Pathway analysis of protein electron­transfer reactions. Annu. Rev. Biophys. Biomol. Struct. 21, 349-377.
  65. Ortiz de Montellano, P.R. (1995) Arylhydrazines as probes of hemoprotein structure and function. Biochimie 77, 581-593.
  66. Osborne, M.J., Crowe, D., Davy, S.L., Macdonald, C. and Moore, G.R. (1997) NMR of paramagnetic proteins. Methods Mol. Biol. 60, 233-269.
  67. Peisach, J., Blumberg, W.E., Ogawa, S., Rachmilewitz, E.A. and Oltzik, R. (1971) The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance. J. Biol. Chem. 246, 3342-3355
  68. Pereira, I.A.C., Teixeira, M. and Xavier, A.V. (1998) Hemeproteins in anaerobes. Structure and Bonding 91, 65-89.
  69. Postnikova, G.B. (1996) Conformation properties of heme­containing proteins using spin labels. Biokhimiia (Moscow) 61, 947-967.
  70. Poulos, T.L. (1988a) Heme enzyme crystal structures. In Eichhorn, G.L. and Marzilli, L.G., Eds. Advances in Inorganic Biochemistry, vol. 7: Heme Proteins. Elsevier, New York, pp. 1-36.
  71. Poulos, T.L. (1996) The role of the proximal ligand in heme enzymes. J. Biol. Inorg. Chem. 1, 356-359.
  72. Ravikanth, M. and Chandrashekar, T.K. (1995) Nonplanar porphyrins and their biological relevance: Ground and excited state dynamics. Structure and Bonding 82, 105-188.
  73. Reiter, W.A., Gerges, A., Lee, S., Deffo, T., Clifford, T., Danby, A. and Bowman­James, K.M. (1998) Accordion porphyrins: Hybrid models for heme and binuclear monooxygenases. Coord. Chem. Rev. 174, 343-359.
  74. Rietjens, I.M.C.M., Osman, A.M., Veeger, C., Zakharieva, O., Antony, J., Grodzicki, M. and Trautwein, A.X. (1996) On the role of the axial ligand in heme­based catalysis of the peroxidase and P450 type. J. Biol. Inorg. Chem. 1, 372-376.
  75. Rifkind, J.M., Abugo, O., Levy, A. and Heim, J. (1994) Detection, formation, and relevance of hemichromes and hemochromes. Methods Enzymol. 231, 449-480.
  76. Rodgers, K.R. (1999) Heme­based sensors in biological systems. Curr. Opin. Chem. Biol. 3, 158-167.
  77. Rose, E., Lecas, A., Quelquejeu, M., Kossanyi, A. and Boitrel, B. (1998) Synthesis of biomimetic heme precursors. Coord. Chem. Rev. 178-180, 1407-1431.
  78. Rothgeb, T.M. and Oldfield, E. (1981) Nuclear magnetic resonance of heme protein crystals. General aspects. J. Biol. Chem. 256, 1432-1446.
  79. Rovira, C. and Parrinello, M. (1999) Factors influencing ligand­binding properties of heme models: A first principles study of picket­fence and protoheme complexes. Chem. Eur. J. 5, 250-262. Computation
  80. Scherer, S. (1990) Do photosynthetic and respiratory electron transport chains share redox proteins? Trends Biochem. Sci. 15, 458-462.
  81. Schweiger, A. (1982) Electron nuclear double resonance of transition metal complexes with organic ligands. Structure and Bonding 51, 1-119.
  82. Schweitzer­Stenner, R. (1989) Allosteric linkage­induced distortions of the prosthetic group in haem proteins as derived by the theoretical interpretation of the depolarization ratio in resonance Raman scattering. Q. Rev. Biophys. 22, 381-479.
  83. Sheldon, R.A. (1994) Oxidation catalysis by metalloporphyrins: A historical perspective. In Sheldon, R.A., Ed. Metalloporphyrins in Catalytic Oxidations. Marcel Dekker, Inc., New York, pp. 1-27.
  84. Shokhirev, N.V. and Walker, F.A. (1998) The effect of axial ligand plane orientation on the contact and pseudocontact shifts of low­spin ferriheme proteins. J. Biol. Inorg. Chem. 3, 581-594. Spectroscopy
  85. Smith, D.W. and Williams, R.J.P. (1970) The spectra of ferric haems and haemoproteins. Structure and Bonding 7, 1-45.
  86. Smith, W.E. (1993) Surface­enhanced resonance Raman scattering. Methods Enzymol. 226, 482-495.
  87. Sono, M., Roach, M.P., Coulter, E.D. and Dawson, J.H. (1996) Heme­containing oxygenases. Chem. Rev. 96, 2841-2887.
  88. Spiro, T.G. (1985) Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. Adv. Protein Chem. 37, 111-159.
  89. Spiro, T.G. and Kozlowski, P.M. (1997) Will the real FeCO please stand up? J. Biol. Inorg. Chem. 2, 516-520.
  90. Spiro, T.G. and Kozlowski, P.M. (1998) Discordant results on FeCO deformability in heme proteins reconciled by density functional theory. J. Am. Chem. Soc. 120, 4524-4525.
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  92. Stouthamer, A.H. (1991) Metabolic regulation including anaerobic metabolism in Paracoccus denitrificans. J. Bioenerg. Biomembr. 23, 163-185.
  93. Telford, J.R., Wittung­Stafshede, P., Gray, H.B. and Winkler, J.R. (1998) Protein folding triggered by electron transfer. Acc. Chem. Res. 31, 755-763.
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  95. Trautwein, A.X. (1974) Mössbauer spectroscopy on heme proteins. Structure and Bonding 20, 101-167.
  96. Trautwein, A.X., Bill, E., Bominaar, E.L. and Winkler, H. (1991) Iron­containing proteins and related analogs - Complementary Mössbauer, EPR and magnetic susceptibility studies. Structure and Bonding 78, 1-96.
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  98. Vangberg, T., Bocian, D.F. and Ghosh, A. (1997) Deformability of Fe(II)CO and Fe(III)CN groups in heme protein models: Nonlocal density functional theory calculations. J. Biol. Inorg. Chem. 2, 526-530. Computation
  99. Varotsis, C. and Babcock, G.T. (1993) Nanosecond time­resolved resonance Raman spectroscopy. Methods Enzymol. 226, 409-431.
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  104. Williams, R.J.P. (1991) Uncoupled and coupled electron transfer reactions. Biochim. Biophys. Acta 1058, 71-74.
  105. Wood, P.M. (1984) Bacterial proteins with CO­binding b­ or c­type haem. Functions and absorption spectroscopy. Biochim. Biophys. Acta 768, 293-317.
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Books

  1. Metal Complexes with Tetrapyrrole Ligands I (1987) Structure and Bonding 64.
  2. Buchler, J.W., Ed. (1991) Metal Complexes with Tetrapyrrole Ligands II. Structure and Bonding 74.
  3. Buchler, J.W., Ed. (1995) Metal Complexes with Tetrapyrrole Ligands III. Structure and Bonding 84.
  4. The Biosynthesis of the Tetrapyrrole Pigments - Symposium No. 180 (1994). CIBA Foundation Symposium Series.
  5. Crichton, R.R. (1991) Inorganic Biochemistry of Iron Metabolism. Ellis Horwood, New York.
  6. Dailey, H.A., Ed. (1990) Biosynthesis of Heme and Chlorophylls. McGraw­Hill, New York.
  7. Jordan, P.M., Ed. (1991) Biosynthesis of Tetrapyrroles. Elsevier, Amsterdam.
  8. Kräutler, B., Golding, B.T. and Arigoni, D., Eds. (1998) Vitamin B12 and B12­Proteins. Wiley-VCH, Weinheim.
  9. Sheldon, R.A., Ed. (1994) Metalloporphyrins in Catalytic Oxidations. Marcel Dekker, Inc., New York.

Nobel Prizes

  1. Deisenhofer, J., Huber, R. and Michel, H. (Chemistry 1988) "for the determination of the three­dimensional structure of a photosynthetic reaction centre".
  2. Fischer, H. (Chemistry 1930) "for his researches into the constitution of haemin and chlorophyll and especially for his synthesis of haemin".
  3. Perutz, M.F. and Kendrew, J.C. (Chemistry 1962) "for their studies of the structures of globular proteins".
  4. Theorell, A.H.T. (Physiology or Medicine 1955) "for his discoveries concerning the nature and mode of action of oxidation enzymes".
  5. Warburg, O.H. (Physiology or Medicine 1931) "for his discovery of the nature and mode of action of the respiratory enzyme".
Reviews on: Structural studies of: