Proteins in electric fields and pressure fields: Experimental results

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1386, Issue 2, 1998, Pages 289-303

  Fidy, J ^a   Balog, E ^a   Kohler M ^b  

^a SEMMELWEIS UNIVERSITY OF MEDICINE   (Hungary)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Conventional Stark spectroscopy; Pressure tuning hole burning spectroscopy; Protein; Stark effect hole burning

Indexed keywords

BACTERIORHODOPSIN; HEMOPROTEIN;

CHROMATOPHORE; ELECTRIC FIELD; PRESSURE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; REVIEW; SPECTROSCOPY; THERMODYNAMICS;

BACTERIORHODOPSINS; ELECTRICITY; HEMEPROTEINS; HORSERADISH PEROXIDASE; HYDROSTATIC PRESSURE; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; PROTEINS; SPECTROPHOTOMETRY;

EID: 0031705781     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00099-5     Document Type: Review

References (68)

1. Friedrich J., Fidy J., Köhler M. Proteins in electric fields: basic aspects. Biochim. Biophys. Acta. 1386:1998;255-288.
2. R.I. Personov, Site selection spectroscopy of complex molecules in solutions and its applications, in: V.M. Agranovich, R.M. Hochstrasser (Eds.), Spectroscopy and Excitation Dynamics of Condensed Molecular Systems, Elsevier, Amsterdam, 1983, pp. 555-619.
3. Champion P.M., Lange R. On the quantitation of light emission from cytochrome c in the low quantum yield limit. J. Chem. Phys. 73:1980;5947-5957.
4. Zollfrank J., Friedrich J., Fidy J., Vanderkooi J.M. Photochemical holes under pressure: compressibility and volume fluctuations of a protein. J. Chem. Phys. 94:1991;8600-8603.
5. Zollfrank J., Friedrich J. Spectral holes under pressure: proteins and glasses. Opt. Soc. Am. B. 9:1991;956-961.
6. Zollfrank J., Friedrich J., Parak F. Spectral hole burning study of protoporphyrin IX substituted myoglobin. Biophys. J. 61:1992;716-724.
7. Gafert J., Friedrich J., Parak F. A comparative pressure tuning hole burning study of protoporphyrin IX in myoglobin and in a glassy host. J. Chem. Phys. 99:1993;2478-2486.
8. Gafert J., Friedrich J., Parak F. Stark-effect experiments on photochemical holes in chromoproteins: protoporphyrin IX substituted myoglobin. Proc. Natl. Acad. Sci. USA. 92:1995;2116-2120.
9. Köhler M., Gafert J., Friedrich J., Vanderkooi J.M., Laberge M. Stark effect experiments in cytochrome c-types proteins: structural hierarchies. Biophys. J. 71:1996;77-85.
10. Köhler M., Gafert J., Friedrich J., Falk H., Meyer J. Hole burning spectroscopy of proteins in external fields: human serum albumin complexed with the hypericinate ion. J. Phys. Chem. 100:1996;8567-8572.
11. Fidy J., Vanderkooi J.M., Zollfrank J., Friedrich J. Softening of the packing density of horseradish peroxidase by a H-donor bound near the heme pocket. Biophys. J. 63:1992;1605-1612.
12. Gafert J., Friedrich J., Parak F., Fidy J. Hole burning and pressure phenomena in chromoproteins. J. Lumin. 56:1993;157-164.
13. Gafert J., Friedrich J., Vanderkooi J.M., Fidy J. Correlation between protein conformation and prosthetic group configuration as tested by pH effects: a hole burning study on mesoporphyrin-IX substituted horseradish peroxidase. J. Phys. Chem. 98:1994;2210-2214.
14. Friedrich J., Gafert J., Zollfrank J., Vanderkooi J.M., Fidy J. Spectral hole burning and selection of conformational substrates in chromoproteins. Proc. Natl. Acad. Sci. USA. 91:1994;1029-1033.
15. Gafert J., Friedrich J., Vanderkooi J.M., Fidy J. Structural changes and internal fields in proteins: a hole-burning Stark effect study of horseradish peroxidase. J. Phys. Chem. 99:1995;5223-5227.
16. Balog E., Kis-Petik K., Fidy J., Köhler M., Friedrich J. Interpretation of multiple Q(0,0) bands in the absorption spectrum of Mg-mesoporphyrin embedded in horseradish peroxidase. J. Biophys. J. 73:1997;397-405.
17. Köhler M., Friedrich J., Balog E., Fidy J. Symmetry breaking by the heme pocket in horseradish peroxidase as revealed by Stark spectroscopy. Chem. Phys. Lett. 277:1997;417-422.
18. Fidy J., Paul K.-G., Vanderkooi J.M. Differences in the binding of aromatic substrates to horseradish peroxidase revealed by fluorescence line narrowing. Biochemistry. 28:1989;7531-7541.
19. Fidy J., Paul K.-G., Vanderkooi J.M. The mechanism of phototautomerization in mesoporphyrin horseradish peroxidase. Studies by fluorescence line narrowing spectroscopy. J. Phys. Chem. 93:1989;2253-2261.
20. Brunet J.E., Jullian C., Jameson D.M. Oxygen diffusion through horseradish peroxidase. Photochem. Photobiol. 51:1990;487-489.
21. Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L. Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nature Struct. Biol. 4:1997;1032-1038.
22. Horie T., Vanderkooi J.M., Paul K.G. Study of the active site of horseradish peroxidase isoenzymes A and C by luminescence. Biochemistry. 24:1985;7935-7941.
23. He X.M., Carter D.C. Atomic structure and chemistry of human serum albumin. Nature. 358:1992;209-215.
24. Takano T. Structure of myoglobin refined at 2.0 Å resolution. II. Structure of deoxymyoglobin from sperm whale. J. Mol. Biol. 110:1977;569-584.
25. Bushnell G.W., Louie G.V., Brayer G.D. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214:1990;585-595.
26. Völker S., van der Waals J.H. Laser-induced photochemical isomerization of free base porphyrin in an n-octane crystal at 4.2K. Mol. Phys. 32:1976;1703-1718.
27. Völker S., Macfarlane R.M. Laser photochemistry and hole burning of chlorin in crystalline n-alkanes at low temperature. J. Chem. Phys. 73:1980;4476-4482.
28. Fidy J., Vanderkooi J.M., Zollfrank J., Friedrich J. More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. Biophys. J. 61:1992;381-391.
29. L. Herenyi, A. Suisalu, K. Mauring, K. Kis-Petik, J. Fidy, J. Kikas, Variety in coupling of a prosthetic group to the apoprotein; studying by energy selected fluorescence excitation and vibronic hole burning spectroscopy, Phys. Chem., in press.
30. P.W. Atkins, Molecular Quantum Mechanics, Oxford University Press, Oxfored, 1983, pp. 349-355.
31. M. Köhler Ph.D. thesis, Techn. Univ. München, 1998.
32. Cowan J.A., Gray H.B. Q-band splitting in the spectra of heme proteins. Inorg. Chem. 28:1989;4554-4556.
33. La Mar G.N., Toi H., Krishnamoorthi R. Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: evidence for intramolecular reorientation about a heme twofold axis. J. Am. Chem. Soc. 106:1984;6395-6401.
34. Bersuker I.B., Stavrov S.S. Structure and properties of metalloporphyrins and hemoproteins: the vibronic approach. Coord. Chem. Rev. 88:1988;1-68.
35. Reddy K.S., Angiolillo P.J., Wright W.W., Laberge M., Vanderkooi J.M. Spectral splitting in the Q(0,0) absorption band of ferrous cytochrome c and other heme proteins. Biochemistry. 35:1996;12820-12830.
36. Kaposi A.D., Fidy J., Stavrov S.S., Vanderkooi J.M. Optical fine-structure investigation of porphyrin-protein interactions: magnesium and metal-free myoglobin. J. Phys. Chem. 97:1993;6319-6327.
37. Fidy J., Laberge M., Kaposi A.D., Vanderkooi J.M. Fluorescence line narrowing applied to the study of proteins. Biochim. Biophys. Acta. 1386:1998;331-351.
38. Sakurada J., Takahashi S., Hosoya T. Nuclear magnetic resonance studies on the relationship of aromatic donor molecules to the heme iron of horseradish peroxidase. J. Biol. Chem. 261:1986;9657-9662.
39. Geissinger P., Kohler B.E., Woehl J.C. Electric field structure in the myoglobin heme pocket. J. Phys. Chem. 99:1995;16527-16529.
40. Middendorf T.R., Mazzola L.T., Lao K., Steffen M.A., Boxer S.G. Stark effect (electroabsorption) spectroscopy of photosynthetic reaction centers at 1.5K: evidence that the special pair has a large excited-state polarizability. Biochim. Biophys. Acta. 1143:1993;223-234.
41. S.G. Boxer, Stark spectroscopy of photosynthetic systems, in: J. Amesz, A.J. Hoff (Eds.), Biophysical Techniques in Photosynthesis, Kluwer Academic, Dordrecht, 1996, pp. 177-189.
42. Bublitz G.U., Boxer S.G. Stark spectroscopy: applications in chemistry, biology and materials science. Annu. Rev. Phys. Chem. 48:1997;213-242.
43. Chance B., Smith L. Respiratory pigments of Rhodospirillum rubrum. Nature. 175:1955;803.
44. Gottfried D.S., Steffen M.A., Boxer S.G. Large protein-induced dipoles for a symmetric carotenoid in a photosynthetic antenna complex. Science. 251:1991;662-665.
45. Gottfried D.S., Steffen M.A., Boxer S.G. Stark effect spectroscopy of carotenoids in photosynthetic antenna and reaction center complexes. Biochim. Biophys. Acta. 1059:1991;76-90.
46. Gottfried D.S., Stocker J.W., Boxer S.G. Stark effect spectroscopy of bacteriochlorophyll in light-harvesting complexes from photosynthetic bacteria. Biochim. Biophys. Acta. 1059:1991;63-75.
47. Lockhart D.J., Boxer S.G. Electric field modulation of the fluorescence from Rhodobacter sphaeroides reaction centers. Chem. Phys. Lett. 144:1988;243-250.
48. Krawczyk S., Maksymiec W. Stark effect in P700, the primary electron donor of Photosystem I. FEBS Lett. 286:1991;110-112.
49. Lockart D.J., Boxer S.G. Stark effect spectroscopy of Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers. Proc. Natl. Acad. Sci. USA. 85:1988;107-111.
50. Lösche M., Feher G., Okamura M.Y. The Stark effect in reaction centers from Rhodobacter sphaeroides R-26 and Rhodopseudomonas viridis. Proc. Natl. Acad. Sci. USA. 84:1987;7537-7541.
51. Prince D.W., Boxer S.G. Stark effect spectroscopy of tryptophan. Biophys. J. 68:1995;1583-1591.
52. Heim R., Prasher D.C., Tsien R.Y. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc. Natl. Acad. Sci. USA. 91:1994;12501-12504.
53. Ward W.W., Bokman S.H. Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renaturated protein. Biochemistry. 21:1982;4535-4540.
54. Chattoraj M., King B.A., Bublitz G.U., Boxer S.G. Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer. Proc. Natl. Acad. Sci. USA. 93:1996;8362.
55. Rees D.C., Chirino A.J., Kim K.H., Komiya H. Membrane proteins structure and stability: implications of the first crystallographic analyses. Methods Physiol. 1:1944;3-26.
56. Hong F.T. Retinal proteins in photovoltaic devices. Adv. Chem. Ser. 240:1944;527-559.
57. D96N. J. Phys. Chem. 96:1992;4679-4685.
58. Trissl H.-W. Photoelectric measurements of purple membranes. Photochem. Photobiol. 51:1990;793-818.
59. Lanyi J.K., Varo Gy. The photocycles of bacteriorhodopsin. Isr. J. Chem. 35:1995;365-385.
60. Keszthelyi L. Orientation of membrane fragments by electric field. Biochim. Biophys. Acta. 598:1980;429-436.
61. Barabas K., Der A., Dancshazy Z., Ormos P., Keszthelyi L., Marden M. Electro-optical measurements on aqueous suspension of purple membrane from Halobacterium halobium. Biophys. J. 43:1983;5-11.
62. Kimura Y., Fujiwara M., Ikegami A. Anisotropic electric properties of purple membrane and their change during the photoreaction cycle. Biophys. J. 45:1984;615-625.
63. Papp E., Fricsovszky G., Meszena G. Electrodichroism of purple membrane. Ionic strength dependence. Biophys. J. 49:1986;1089-1100.
64. Tjusi K., Neumann E. Conformational flexibility of membrane proteins in electric fields. I. Ultraviolet absorbance and light scattering of bacteriorhodopsin in purple membranes. Biophys. Chem. 17:1983;153-163.
65. Gerwert K., Souvignier G., Hess B. Simultaneous monitoring of light-induced changes in protein side-group protonation chromophore isomerization and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform IR spectroscopy. Proc. Natl. Acad. Sci. USA. 87:1990;9774-9778.
66. Koch M.H., Dencher N.A., Oesterhelt D., Plohn H.J., Rapp G., Buldt G. Time-resolved x-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10:1991;521-526.
67. Kimura Y., Vassylyev D.G., Miayazawa A., Kidera A., Matsushima M., Mitsuoka K., Murata K., Hirai T., Fujiyoshi Y. Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature. 389:1997;206-211.
68. Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.