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Bibliography on structural studies of cytochrome b5 family

  1. Altman, J., Lipka, J.J., Kuntz, I.D. and Waskell, L. (1989) Identification by proton nuclear magnetic resonance of the histidines in cytochrome b5 modified by diethyl pyrocarbonate. Biochemistry 28, 7516-7523.
  2. Argos, P. and Mathews, F.S. (1975) The structure of ferrocytochrome b5 at 2.8 Å resolution. J. Biol. Chem. 250, 747-751.
  3. Arnesano, F., Banci, L., Bertini, I. and Felli, I.C. (1998a) The solution structure of oxidized rat microsomal cytochrome b5. Biochemistry 37, 173-184.
  4. Arnesano, F., Banci, L., Bertini, I. and Koulougliotis, D. (1998b) Solution structure of oxidized rat microsomal cytochrome b5 in the presence of 2 M guanidinium chloride: Monitoring the early steps in protein unfolding. Biochemistry 37, 17082-17092.
  5. Arnesano, F., Banci, L., Bertini, I., Felli, I.C. and Koulougliotis, D. (1999) Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating­frame NMR­relaxation measurements. Biological implications. Eur. J. Biochem. 260, 347-354.
  6. Banci, L., Pierattelli, R. and Turner, D.L. (1995) Determination of haem electronic structure in cytochrome b5 and metcyanomyoglobin. Eur. J. Biochem. 232, 522-527.
  7. Banci, L., Bertini, I., Ferroni, F. and Rosato, A. (1997) Solution structure of reduced microsomal rat cytochrome b5. Eur. J. Biochem. 249, 270-279.
  8. Banci, L., Bertini, I., Cavazza, C., Felli, I.C. and Koulougliotis, D. (1998a) Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: Biological implications. Biochemistry 37, 12320-12330.
  9. Banci, L., Bertini, I., Huber, J.G., Luchinat, C. and Rosato, A. (1998b) Partial orientation of oxidized and reduced cytochrome b5 at high magnetic fields: Magnetic susceptibility anisotropy contributions and consequences for protein solution structure determination. J. Am. Chem. Soc. 120, 12903-12909.
  10. Barker, P.D., Ferrer, J.C., Mylrajan, M., Loehr, T.M., Feng, R., Konishi, Y., Funk, W.D., MacGillivray, R.T. and Mauk, A.G. (1993) Transmutation of a heme protein. Proc. Natl. Acad. Sci. USA 90, 6542-6546.
  11. Bhattacharya, S., Falzone, C.J. and Lecomte, J.T. (1999) Backbone dynamics of apocytochrome b5 in its native, partially folded state. Biochemistry 38, 2577-2589.
  12. Burch, A.M., Rigby, S.E., Funk, W.D., MacGillivray, R.T., Mauk, M.R., Mauk, A.G. and Moore, G.R. (1990) NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex. Science 247, 831-833.
  13. Capeillèere­Blandin, C., Bray, R.C., Iwatsubo, M. and Labeyrie, F. (1975) Flavocytochrome b2: kinetic studies by absorbance and electron­paramagnetic­resonance spectroscopy of electron distribution among prosthetic groups. Eur. J. Biochem. 54, 549-566.
  14. Constans, A.J., Mayer, M.R., Sukits, S.F. and Lecomte, J.T.L. (1998) A test of the relationship between sequence and structure in proteins: Excision of the heme binding site in apocytochrome b5. Protein Science 7, 1983-1993.
  15. Dangi, B., Sarma, S., Yan, C., Banville, D.L. and Guiles, R.D. (1998a) The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high­resolution NMR structures and backbone dynamic analyses. Biochemistry 37, 8289-8302.
  16. Dangi, B., Blankman, J.I., Miller, C.J., Volkman, B.F. and Guiles, R.D. (1998b) Contribution of backbone dynamics to entropy changes occurring on oxidation of cytochrome b5. Can redox linked changes in hydrogen bond networks modulate reduction potentials? J. Phys. Chem. B102, 8201-8208.
  17. Davydov, R.M., Kariakin, A.V. and Greschner, S. (1980) Absorption spectra and magnetic circular dichroism of ferrocytochrome b5 formed during low temperature reduction in a nonequilibrium state. Biofizika (Moscow) 25, 393-397.
  18. Desbois, A., Tegoni, M., Gervais, M. and Lutz, M. (1989) Flavin and heme structures in lactate:cytochrome c oxidoreductase: A resonance Raman study. Biochemistry 28, 8011-8022.
  19. Durley, R.C.E. and Mathews, F.S. (1996) Refinement and structural analysis of bovine cytochrome b5 at 1.5 Å resolution. Acta Crystallogr. D52, 65-76.
  20. Falzone, C.J., Mayer, M.R., Whiteman, E.L., Moore, C.D. and Lecomte, J.T.J. (1996) Design challenges for hemoproteins: The solution structure of apocytochrome b5. Biochemistry 35, 6519-6526.
  21. Funk, W.D., Lo, T.P., Mauk, M.R., Brayer, G.D., MacGillivray, R.T. and Mauk, A.G. (1990) Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b5 oxidation­reduction equilibrium: involvement of asparagine­57, serine­64, and heme propionate­7. Biochemistry 29, 5500-5508.
  22. Gao, Y., Veitch, N.C. and Williams, R.J.P. (1991) The value of chemical shift parameters in the description of protein solution structures. J. Biomol. NMR 1, 457-471.
  23. Gruenke, L.D., Sun, J., Loehr, T.M. and Waskell, L. (1997) Resonance Raman spectral properties and stability of manganese protoporphyrin IX cytochrome b5. Biochemistry 36, 7114-7125.
  24. Guiard, B. and Lederer, F. (1978) Surface differences and similarities in two homologous proteins. Cytochrome b5 and cytochrome b2 core. Biochim. Biophys. Acta 536, 88-96.
  25. Guiles, R.D., Altman, J., Kuntz, I.D., Waskell, L. and Lipka, J.J. (1990) Structural studies of cytochrome b5: Complete sequence­specific resonance assignments for the trypsin­solubilized microsomal ferrocytochrome b5 obtained from pig and calf. Biochemistry 29, 1276-1289.
  26. Guiles, R.D., Basus, V.J., Kuntz, I.D. and Waskell, L. (1992) Sequence­specific 1H and 15N resonance assignments for both equilibrium forms of the soluble heme binding domain of rat ferrocytochrome b5. Biochemistry 31, 11365-11375.
  27. Guiles, R.D., Basus, V.J., Sarma, S., Malpure, S., Fox, K.M., Kuntz, I.D. and Waskell, L. (1993) Novel heteronuclear methods of assignment transfer from a diamagnetic to a paramagnetic protein: application to rat cytochrome b5. Biochemistry 32, 8329-8340.
  28. Guiles, R.D., Sarma, S., DiGate, R.J., Banville, D., Basus, V.J., Kuntz, I.D. and Waskell, L. (1996) Pseudocontact shifts used in the restraint of the solution structures of electron transfer complexes. Nature Struct. Biol. 3, 333-339.
  29. Hartshorn, R.T., Mauk, A.G., Mauk, M.R. and Moore, G.R. (1987) NMR study of the interaction between cytochrome b5 and cytochrome c. Observation of a ternary complex formed by the two proteins and [Cr(en)3]3+. FEBS Lett. 213, 391-395.
  30. Hewson, R., Newbold, R.J. and Whitford, D. (1993) The expression of bovine microsomal cytochrome b5 in Escherichia coli and a study of the solution structure and stability of variant proteins. Protein Engineering 6, 953-964.
  31. Hori, A., Hayashi, F., Kyogoku, Y. and Akutsu, H. (1988) A photo­chemically induced dynamic nuclear polarization NMR study on rabbit and bovine cytochrome b5. Eur. J. Biochem. 174, 503-508.
  32. Hunter, C.L., Lloyd, E., Eltis, L.D., Rafferty, S.P., Lee, H., Smith, M. and Mauk, A.G. (1997) Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5. Biochemistry 36, 1010-1017.
  33. Keller, R.M. and Wüthrich, K. (1980) Structural study of the heme crevice in cytochrome b5 based on individual assignments of the 1H­NMR lines of the heme group and selected amino acid residues. Biochim. Biophys. Acta 621, 204-217.
  34. Keller, R.M., Groudinsky, O. and Wüthrich, K. (1976) Contact-shifted resonances in the 1H NMR spectra of cytochrome b5. Resonance identification and spin density distribution in the heme group. Biochim. Biophys. Acta 427, 497-511.
  35. Kelly, G.P., Muskett, F.W. and Whitford, D. (1997) Analysis of backbone dynamics in cytochrome b5 using 15N­NMR relaxation measurements. Eur. J. Biochem. 245, 349-354.
  36. Labeyrie, F., Beloeil, J.C. and Thomas, M.A. (1988) Evidence by NMR for mobility of the cytochrome domain within flavocytochrome b2. Biochim. Biophys. Acta 953, 134-141.
  37. Lee, K.B., La Mar, G.N., Kehres, L.A., Fujinari, E.M., Smith, K.M., Pochapsky, T.C. and Sligar, S.G. (1990) 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5. Biochemistry 29, 9623-9631.
  38. Lee, K.B., La Mar, G.N., Pandey, R.K., Rezzano, I.N., Mansfield, K.E. and Smith, K.M. (1991) 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5. Biochemistry 30, 1878-1887.
  39. Lee, K.B., La Mar, G.N., Mansfield, K.E., Smith, K.M., Pochapsky, T.C. and Sligar, S.G. (1993) Interpretation of hyperfine shift patterns in ferricytochromes b5 in terms of angular position of the heme: a sensitive probe for peripheral heme protein interactions. Biochim. Biophys. Acta 1202, 189-199.
  40. Lee, K.B., McLachlan, S.J. and La Mar, G.N. (1994) Hydrogen isotope effects on the proton nuclear magnetic resonance spectrum of bovine ferricytochrome b5: Axial hydrogen bonding involving the axial His­39 imidazole ligand. Biochim. Biophys. Acta 1208, 22-30.
  41. Livingston, D.J., McLachlan, S.J., La Mar, G.N. and Brown, W.D. (1985) Myoglobin:cytochrome b5 interactions and the kinetic mechanism of metmyoglobin reductase. J. Biol. Chem. 260, 15699-15707.
  42. Lloyd, E., Ferrer, J.C., Funk, W.D., Mauk, M.R. and Mauk, A.G. (1994) Recombinant human erythrocyte cytochrome b5. Biochemistry 33, 11432-11437.
  43. McLachlan, S.J., La Mar, G.N., Burns, P.D., Smith, K.M. and Langry, K.C. (1986) 1H­NMR assignments and the dynamics of interconversion of the isomeric forms of cytochrome b5 in solution. Biochim. Biophys. Acta 874, 274-284.
  44. Mathews, F.S. (1980) The orientation of the heme group in crystalline cytochrome b5. Biochim. Biophys. Acta 622, 375-379.
  45. Mathews, F.S., Argos, P. and Levine, M. (1972) The structure of cytochrome b5 at 2.0 Angstrom resolution. Cold Spring Harbor Symp. Quant. Biol. 36, 387-395.
  46. Moore, C.D. and Lecomte, J.T. (1990) Structural properties of apocytochrome b5: presence of a stable native core. Biochemistry 29, 1984-1989.
  47. Muskett, F.W., Kelly, G.P. and Whitford, D. (1996) The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods. J. Mol. Biol. 258, 172-189.
  48. Qian, W., Sun, Y.­L., Wang, Y.­H., Zhuang, J.­H., Xie, Y. and Huang, Z.­X. (1998) The influence of mutation at Glu44 and Glu56 of cytochrome b5 on the protein's stabilization and interaction between cytochrome c and cytochrome b5. Biochemistry 37, 14137-14150.
  49. Qiao, T., Witkowski, R., Henderson, R. and McLendon, G. (1996) Kinetic studies of electron transfer in the cyt b5:metHb system. J. Biol. Inorg. Chem. 1, 432-438.
  50. Reid, L.S., Gray, H.B., Dalvit, C., Wright, P.E. and Saltman, P. (1987) Electron transfer from cytochrome b5 to iron and copper complexes. Biochemistry 26, 7102-7107.
  51. Rivera, M., Barillas­Mury, C., Christensen, K.A., Little, J.W., Wells, M.A. and Walker, F.A. (1992) Gene synthesis, bacterial expression, and 1H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b5. Biochemistry 31, 12233-12240.
  52. Rivera, M., Wells, M.A. and Walker, F.A. (1994) Cation­promoted cyclic voltammetry of recombinant rat outer mitochondrial membrane cytochrome b5 at a gold electrode modified with ß­mercaptopropionic acid. Biochemistry 33, 2161-2170.
  53. Rivera, M., Qiu, F., Bunce, R.A. and Stark, R.E. (1999) Complete isomer­specific 1H and 13C NMR assignments of the heme resonances of rat liver outer mitochondrial membrane cytochrome b5. J. Biol. Inorg. Chem. 4, 87-98.
  54. Rodríguez, J.C. and Rivera, M. (1998) Conversion of mitochondrial cytochrome b5 into a species capable of performing the efficient coupled oxidation of heme. Biochemistry 37, 13082-13090.
  55. Rodríguez­Marañón, M.J., Qiu, F., Stark, R.E., White, S.P., Zhang, X., Foundling, S.I., Rodríguez, V., Schilling, C.L., III, Bunce, R.A. and Rivera, M. (1996) 13C NMR spectroscopic and X­ray crystallographic study of the role played by mitochondrial cytochrome b5 heme propionates in the electrostatic binding to cytochrome c. Biochemistry 35, 16378-16390.
  56. Rossmann, M.G. and Argos, P. (1975) A comparison of the heme binding pocket in globins and cytochrome b5. J. Biol. Chem. 250, 7525-7532.
  57. Sarma, S., DiGate, R.J., Banville, D.L. and Guiles, R.D. (1996) 1H, 13C and 15N NMR assignments and secondary structure of the paramagnetic form of rat cytochrome b5. J. Biomol. NMR 8, 171-183.
  58. Sarma, S., Dangi, B., Yan, C., DiGate, R.J., Banville, D.L. and Guiles, R.D. (1997a) Characterization of a site­directed mutant of cytochrome b5 designed to alter axial imidazole ligand plane orientation. Biochemistry 36, 5645-5657.
  59. Sarma, S., DiGate, R.J., Goodin, D.B., Miller, C.J. and Guiles, R.D. (1997b) Effect of axial ligand plane reorientation on electronic and electrochemical properties observed in the A67V mutant of rat cytochrome b5. Biochemistry 36, 5658-5668.
  60. Sun, Y.­L., Xie, Y., Wang, Y.­H., Xiao, G.­T. and Huang, Z.­X. (1996) The influence of Glu44 and Glu56 of cytochrome b5 on the protein structure and interaction with cytochrome c. Protein Engineering 9, 555-558.
  61. Sun, Y.­L., Wang, Y.­H., Yan, M.­M., Sun, B.­Y., Xie, Y., Huang, Z.­X., Jiang, S.­K. and Wu, H.­M. (1999) Structure, interaction and electron transfer between cytochrome b5, its E44A and/or E56A mutants and cytochrome c. J. Mol. Biol. 285, 347-359.
  62. Tegoni, M. and Cambillau, C. (1994a) Structural studies on recombinant and point mutants of flavocytochrome b2. Biochimie 76, 501-514.
  63. Tegoni, M. and Cambillau, C. (1994b) The 2.6­Å refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex. Protein Science 3, 303-313.
  64. Tegoni, M., Mozzarelli, A., Rossi, G.L. and Labeyrie, F. (1983) Complex formation and intermolecular electron transfer between flavocytochrome b2 in the crystal and cytochrome c. J. Biol. Chem. 258, 5424-5427.
  65. Tegoni, M., Begotti, S. and Cambillau, C. (1995) X­ray structure of two complexes of the Y143F flavocytochrome b2 mutant crystallized in the presence of lactate or phenyl lactate. Biochemistry 34, 9840-9850.
  66. Tegoni, M., Gervais, M. and Desbois, A. (1997) Resonance Raman study on the oxidized and anionic semiquinone forms of flavocytochrome b2 and L­lactate monooxygenase. Influence of the structure and environment of the isoalloxazine ring on the flavin function. Biochemistry 36, 8932-8946.
  67. Veitch, N.C., Concar, D.W., Williams, R.J.P. and Whitford, D. (1988) Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy. FEBS Lett. 238, 49-55.
  68. Veitch, N.C., Whitford, D. and Williams, R.J.P. (1990) An analysis of pseudocontact shifts and their relationship to structural features of the redox states of cytochrome b5. FEBS Lett. 269, 297-304.
  69. Wei, X., Ming, L.J., Cannons, A.C. and Solomonson, L.P. (1998) 1H and 13C NMR studies of a truncated heme domain from Chlorella vulgaris nitrate reductase: Signal assignment of the heme moiety. Biochim. Biophys. Acta 1382, 129-136
  70. Whitford, D. (1992) The identification of cation­binding domains on the surface of microsomal cytochrome b5 using 1H­NMR paramagnetic difference spectroscopy. Eur. J. Biochem. 203, 211-223.
  71. Whitford, D., Concar, D.W., Veitch, N.C. and Williams, R.J.P. (1990) The formation of protein complexes between ferricytochrome b5 and ferricytochrome c studied using high­resolution 1H­NMR spectroscopy. Eur. J. Biochem. 192, 715-721.
  72. Whitford, D., Gao, Y., Pielak, G.J., Williams, R.J.P., McLendon, G.L. and Sherman, F. (1991) The role of the internal hydrogen bond network in first­order protein electron transfer between Saccharomyces cerevisiae iso­1­cytochrome c and bovine microsomal cytochrome b5. Eur. J. Biochem. 200, 359-367.
  73. Yao, P., Xie, Y., Wang, Y.­H., Sun, Y.­L., Huang, Z.­X., Xiao, G.­T. and Wang,, S.­D. (1997) Importance of a conserved phenylalanine­35 of cytochrome b5 to the protein's stability and redox potential. Protein Engineering 10, 575-581.
  74. Xia, Z.X. and Mathews, F.S. (1990) Molecular structure of flavocytochrome b2 at 2.4 Å resolution. J. Mol. Biol. 212, 837-863.
  75. Xia, Z.X., Shamala, N., Bethge, P.H., Lim, L.W., Bellamy, H.D., Xuong, N.H., Lederer, F. and Mathews, F.S. (1987) Three­dimensional structure of flavocytochrome b2 from baker's yeast at 3.0­Å resolution. Proc. Natl. Acad. Sci. USA 84, 2629-2633.
Reviews on cytochrome b5 family