1H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c

Journal of Biochemistry

Volumn 119, Issue 1, 1996, Pages 16-22

  Yamamoto, Yasuhiko ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

Curie plot; Cytochrome c; Hemoprotein; Hyperfine shift; NMR

Indexed keywords

EQUUS CABALLUS;

CYTOCHROME C; HEMOPROTEIN;

ARTICLE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HORSE; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; TEMPERATURE DEPENDENCE;

ANIMALS; BINDING SITES; CYTOCHROME C GROUP; HEME; HISTIDINE; HORSES; IMIDAZOLES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MYOCARDIUM; PROTONS; TEMPERATURE;

EID: 0029671189     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021202     Document Type: Article

References (61)

1. La Mar, G.N. (1973) Model compounds as aids in interpreting NMR spectra of hemoproteins in Biological Applications of Magnetic Resonance (Shulman, R.G., ed.) pp. 305-343, Academic Press, New York
2. Satterlee, J.D. (1986) NMR spectroscopy of paramagnetic haem proteins. Annu. Rep. NMR Spectrosc. 17, 79-178
3. Satterlee, J.D. (1986) Proton NMR studies of biological problems involving paramagnetic heme proteins. Met. Ions Biol. Syst. 21, 121-185
4. Shulman, R.G., Glarum, S.H., and Karplus, M. (1971) Electronic structure of cyanide complexes of hemes and heme proteins. J. Mol. Biol. 57, 93-115
5. Traylor, T.G. and Berzinis, A.P. (1980) Hemoprotein models: NMR of imidazole chelated protohemin cyanide complexes. J. Am. Chem. Soc. 102, 2844-2846
6. Smith, M. and McLendon, G. (1981) Comparative NMR studies of cytochrome c and its active site octapeptide. J. Am. Chem. Soc. 103, 4912-4921
7. Yamamoto, Y., Nanai, N., Chujo, R., and Suzuki, T. (1990) Heme methyl hyperfine shift pattern as a probe for determining the orientation of the functionally relevant proximal histidyl imidazole with respect to the heme in hemoproteins. FEBS Lett. 264, 113-116
8. Neya, S. and Funasaki, N. (1987) Proton NMR study of the cyanide metmyoglobin reconstituted with meso-tetraalkyl-hemins. Dynamic free rotation of the synthetic hemins in the heme pocket. J. Biol. Chem. 262, 6725-6728
9. Peyton, D.H., LaMar, G.N., Pande, U., Ascoli, F., Smith, K.M., Pandey, R.K., Parish, D.W., Bolognesi, M., and Brunori, M. (1989) Proton nuclear magnetic resonance study of the molecular and electronic structure of the heme cavity in Aplysia cyanometmyoglobin. Biochemistry 28, 4880-4887
10. Yamamoto, Y. and Suzuki, T. (1993) NMR study of the molecular and electronic structure of the heme cavity in Dolabella metcyano myoglobin. Biochim. Biophys. Acta 1163, 287-296
11. 1H Fermi contact shifts in horse cytochrome c. The origin of the anti-Curie effect. Eur. J. Biochem. 211, 563-568
12. Beetlestone, J. and George, P. (1964) A magnetochemical study of equilibria between high and low spin states of metmyoglobin complexes. Biochemistry 3, 707-714
13. Iizuka, T. and Kotani, M. (1968) A thermal equilibrium between high- and low-spin states in ferric cytochrome c peroxidase and some discussion on the enzyme-substrate complex. Biochim. Biophys. Acta 167, 257-267
14. Iizuka, T. and Kotani, M. (1969) Analysis of thermal equilibrium between high-spin and low-spin states in ferrihemoglobin complexes. Biochim. Biophys. Acta 194, 351-363
15. Alben, J.O. and Fager, L.Y. (1972) Infrared studies of azide bound to myoglobin and hemoglobin. Temperature dependence of ionicity. Biochemistry 11, 842-849
16. Iizuka, T. and Morishima, I. (1974) 220 MHz proton NMR studies of hemoprotein. High spin-low spin equilibrium in ferric myoglobin and hemoglobin derivatives. Biochim. Biophys. Acta 371, 1-13
17. Morishima, I., Neya, S., Inubushi, T., Yonezawa, T., and Iizuka, T. (1978) Nuclear magnetic resonance studies of hemoprotein. Proton hyperfine shifts and structural characterization of the different heme environments in methemoglobin and metmyoglobin. Biochim. Biophys. Acta 534, 307-316
18. Neya, S. and Funasaki, N. (1986) Proton nuclear magnetic resonance investigation of the spin-state equilibrium of the Α and β subunits in intact azidomethemoglobin. Biochemistry 25, 1221-1226
19. Yamamoto, Y. and La Mar, G.N. (1989) Proton NMR investigation of the influence of subunit assembly on the low-spins⇄ high-spin equilibrium of met-azido hemoglobin A. Biochim. Biophys. Acta 996, 187-194
20. 1-NMR evidence fora structural alteration on the active site of G. japonicus myoglobin upon azide ion binding. Eur. J. Biochem. 198, 285-291
21. 1H NMR study of labile proton exchange in the heme cavity as a probe for the potential ligand entry channel in myoglobin. Biochemistry 24, 7388-7395
22. Yamamoto, Y., Iwafune, K., Chujo, R., Inoue, Y., Imai, K., and Suzuki, T. (1992) Molecular mechanism for ligand stabilization in the mollusc myoglobin possessing the distal Val residue. J. Mol. Biol. 228, 343-346
23. Yamamoto, Y., Iwafune, K., Nanai, N., Chujo, R., Inoue, Y., and Suzuki, T. (1992) Orientation and mobility of the heme vinyl groups in myoglobins with the aid of NOE and MATDUHM NMR. Biochim. Biophys. Acta 1120, 173-182
24. 1H NMR resonance assignment and dynamic analysis of phenylalanine CD1 in a low-spin ferric complex of sperm whale myoglobin. J. Am. Chem. Soc. 110, 4176-4182
25. Yamamoto, Y. and La Mar, G.N. (1986) NMR study of dynamics and thermodynamics of heme rotational disorder in native and reconstituted hemoglobin A. Biochemistry 25, 5288-5297
26. La Mar, G.N., Toi, H., and Krishnamoorthi, R. (1988) Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: Evidence for intermolecular reorientation about a heme twofold axis. J. Am. Chem. Soc. 110, 4176-4182
27. Neya, S. and Funasaki, N. (1988) Proton NMR study of the myoglobin reconstituted with meso-tetra (n-propyl) hemin. Biochim. Biophys. Acta 952, 150-157
28. Neya, S., Funasaki, N., and Nakamura, N. (1992) Dynamic analysis of efficient heme rotation in myoglobin by NMR spectroscopy. Biochim. Biophys. Acta 1117, 243-250
29. Neya, S., Funasaki, N., Sato, T., Igarashi, N., and Tanaka, N. (1993) Structural analysis of the myoglobin reconstituted with iron porphine. J. Biol. Chem. 268, 8935-8942
30. 1H NMR study of the role of individual heme propionates in modulating structural and dynamic properties of the heme pocket in myoglobin. J. Am. Chem. Soc. 112, 6198-6205
31. Hauksson, J.B., La Mar, G.N., Pandey, R.K., Rezzano, I.N., and Smith, K.M. (1990) NMR study of heme pocket polarity/hydrophobicity of myoglobin using polypropionate-substituted hemins. J. Am. Chem. Soc. 112, 8315-8323
32. La Mar, G.N., Hauksson, J.B., Dugad, L.B., Liddell, P.A., Venkataramana, N., and Smith, K.M. (1991) Proton NMR study of the heme rotational mobility in myoglobin: The role of propionate salt bridges in anchoring the heme. J. Am. Chem. Soc. 113, 1544-1550
33. Takano, T. (1977) Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568
34. Kuriyan, J., Wilz, S., Karplus, M., and Petsko, G.A. (1986) X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution. J. Mol. Biol. 192, 133-154
35. Case, D.A. and Karplus, M. (1979) Dynamics of ligand binding to heme proteins. J. Mol. Biol. 132, 343-368
36. McDonald, C.C. and Phillips, W.D. (1973) Proton magnetic resonance studies of horse cytochrome c. Biochemistry 12, 3170-3186
37. 551 from Pseudomonas aeruginosa. Biochemistry 18, 774-779
38. 2. Biochemistry 18, 1628-1634
39. 1H NMR spectroscopy of Paracoccus denitrificans cytochrome c-550. Biochemistry 23, 3526-3533
40. Jesson, J.P. (1973) The paramagnetic shift in NMR of Paramagnetic Molecules, Principles and Applications (La Mar, G.N., Horrocks, W. Dew., Jr., and Holm, E.H., eds.) pp. 1-52, Academic Press, New York
41. Bertini, I. and Luchinat, C. (1986) NMR of Paramagnetic Molecules in Biological Systems, Chap. 2, Benjamin/Cummings, Menlo Park, CA
42. La Mar, G.N. (1973) Spin delocalization and electronic structure in NMR of Paramagnetic Molecules, Principles and Applications (LaMar, G.N., Horrocks, W. Dew., Jr., and Holm, R.H., eds.) pp. 85-126, Academic Press, New York
43. Goff, H.M. (1981) Iron (III) porphyrin-imidazole complexes. Analysis of carbon-13 nuclear magnetic resonance isotropic shifts and unpaired spin delocalization. J. Am. Chem. Soc. 103, 3714-3722
44. Goff, H.M. (1983) Nuclear magnetic resonance of iron porphyrins in Ion Porphyrins, Part I (Lever, A.B.P. and Gray, H.B., eds.) pp. 237-281, Addison-Wesley Publishing Company, London
45. Satterlee, J.D., La Mar, G.N., and Frye, J.S. (1976) Dynamics and thermodynamics of axial ligation in metalloporphyrins. 5. Affinity of ferric porphyrins for nitrogenous bases and the stoichiometry and spin states of the product complexes. J. Am. Chem. Soc. 98, 7275-7282
46. Satterlee, J.D. and La Mar, G.N. (1976) A proton nuclear magnetic resonance study of imidazole-iron bonding in low-spin ferric complexes with synthetic porphyrins. J. Am. Chem. Soc. 98, 2804-2808
47. La Mar, G.N., de Ropp, J.S., Chako, V.P., Satterlee, J.D., and Erman, J.E. (1982) Axial histidyl imidazole non-exchangeable proton resonances as indicators of imidazole hydrogen bonding in ferric cyanide complexes of heme peroxidases. Biochim. Biophys. Acta 708, 317-325
48. Behere, D.V., Ales, D.C., and Goff, H.M. (1986) Proton and nitrogen-15 NMR studies of ferricytochrome c cyanide complexes: Remarkable conservation of the heme environment among organisms of diverse origin. Biochim. Biophys. Acta 876, 285-292
49. 1NMR spectra of cytochrome c. Biochim. Biophys. Acta 533, 195-208
50. Bushnell, G.W., Louie, G.V., and Brayer, G.D. (1990) High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214, 585-595
51. Berghuis, A.M. and Brayer, G.D. (1992) Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223, 959-976
52. - in ferric low-spin cyanide complexes of various porphyrin derivatives and various hemoproteins. J. Am. Chem. Soc. 100, 3568-3574
53. Behere, D.V., Gonzalez-Vergara, E., and Goff, H.M. (1985) Unique cyanide nitrogen-15 nuclear magnetic resonance chemical shift values for cyano-peroxidase complexes. Relevance to the heme active-site structure and mechanism of peroxide activation. Biochim. Biophys. Acta 832, 319-325
54. La Mar, G.N. and de Ropp, J.S. (1982) Proton NMRcharacterization of the state of protonation of the axial imidazole in reduced horseradish peroxidase. J. Am. Chem. Soc. 104, 5203-5206
55. Emerson, S.D. and La Mar, G.N. (1990) NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin : A new probe of steric tilt of bound ligand. Biochemistry 29, 1556-1566
56. Feng, Y., Roder, H., and Englander, S.W. (1990) Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c. Biochemistry 29, 3494-3504
57. Senn, H. and Wüthrich, K. (1983) Conformation of the axially bound ligands of the heme iron and electronic structure of heme c in the cytochrome c-551 from Pseudomonas mendocina and Pseudomonas stutzeri and in cytochrome C2 from Rhodospirillum rubrum. Biochim. Biophys. Acta 746, 48-60
58. Santos, H. and Turner, D.L. (1986) Carbon-13 and proton NMR studies of horse cytochrome c. Assignment and temperature dependence of methyl resonances. FEBS Lett. 194, 73-77
59. 1NMR spectra of cytochrome c. Biochim. Biophys. Acta 533, 195-208
60. Redfield, A.G. and Gupta, R.K. (1971) Pulsed NMR study of the structure of cytochrome c. Cold Spring Harbor Symp. Quat. Biol. 36, 405-411
61. 13C-NMR studies of horse ferrocytochrome c. Assignment and temperature dependence of methyl resonances. FEBS Lett. 184, 240-244