Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus

European Journal of Biochemistry

Volumn 261, Issue 1, 1999, Pages 325-336

  Agalidis, Ileana ^a,c   Othman, Samya ^b   Boussac, Alain ^a   Reiss Husson, Françoise ^a   Desbois, Alain ^b  

^a CNRS   (France)

^b Dept de Biologie Cell et Molec   (France)

^c DIF   (France)

Author keywords

Absorption; Electron paramagnetic resonance; Purple bacteria; Resonance Raman; Tetraheme cytochrome

Indexed keywords

ASCORBIC ACID; CYTOCHROME C; DIAMINODURENE; DITHIONITE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ISOLATION; ENZYME MODIFICATION; ENZYME PURIFICATION; ENZYME SUBUNIT; NONHUMAN; OXIDATION REDUCTION REACTION; PHOTOTROPHIC BACTERIUM; PRIORITY JOURNAL; REACTION ANALYSIS;

EID: 0033119691     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00277.x     Document Type: Article

References (55)

1. 1. Nitschke, W. & Dracheva, S.M. (1995) Reaction center associated cytochromes. In Anoxygenic Photosynthetic Bacteria (Blankenship, R.E., Madigan, M.T. & Bauer, C.E., eds), pp. 775-805. Kluwer Academic Publishers, Dordrecht.
2. 2. Deisenhofer, J.O., Sinning, I. & Michel, H. (1995) Cristallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J. Mol. Biol. 246, 429-457.
3. 3. Nitschke, W. & Rutherford, A.W. (1989) Tetraheme cytochrome-c subunit of Rhodopseudomonas viridis characterized by EPR. Biochemistry 28, 3161-3168.
4. 4. Nagashima, K.V.P., Matsuura, K., Ohyama, S. & Shimada, K. (1994) Primary structure and transcription of genes encoding B870 and photosynthetic reaction center apoproteins from Rubrivivax gelutinosus. J. Biol. Chem. 269, 2477-2484.
5. 5. Ouchane, S., Picaud, M., Reiss-Husson, F., Vernotte, C. & Astier, C. (1996) Development of genetic transfers for Rubrivivax gelatinosus SI. Construction, characterization and complementation of a puf operon deletion strain. Mol. Genet. Gen. 252, 379-385.
6. 6. Nitschke, W., Agalidis, I. & Rutherford, A.W. (1992) The reaction centre associated cytochrome suhunit of the purple bacterium Rhodocycius gelatinosus. Biochim. Biophys. Acta 1100, 49-57.
7. 7. Garcia, D., Richaud, P. & Vermeglio, A. (1993) The photoinduced cyclic electron transfer in whole cells of Rhodopseudomonas viridis. Biochim. Biophys. Acta 1144, 295-301.
8. 2 with photosynthetic reaction centers from Rhodopseiidomonas viridis. Biochemistry 30, 1303-1310.
9. 9. Meyer, T.E., Bartsch, R.G., Cusanovich, M.A. & Tollin, G. (1993) Kinetics of photooxidation of soluble cytochromes, HiPIP, and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis. Biochemistry 32, 4719-4726.
10. 10. Schoepp, B., Parot, P., Menin, L., Gaillard, J., Richaud, P. & Verméglio, A. (1995) In vivo participation of a high potential iron-sulfur protein as electron donor to the photochemical reaction center of Rubrivivax gelatinosus. Biochemistry 34, 11736-11742.
11. 11. Agalidis, I. & Reiss-Husson, F. (1992) Purification and characterization of Rhodocyclus gelatinosus photochemical reaction center. Biochim. Biophys. Acta 1098, 201-208.
12. 12. Michel, H. (1982) Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from Rhodopseudomonas viridis. J. Mol. Biol. 158, 567-572.
13. 13. Agalidis, I., Rivas, E. & Reiss-Husson, F. (1990) Reaction center-light harvesting B875 complexes from Rhodocyclus gelatinosus -characterization and identification of quinones. Photosynth. Res. 23, 249-255.
14. 14. Ouchane, S., Picaud, M., Vernotte, C., Reiss-Husson, F. & Astier, C. (1997) Pleiotropic effects of puf interposon mutagenesis on carotenoid biosynthesis in Rubrivivax gelatinosus. A new gene organization in purple bacteria. J. Biol. Chem. 272, 1670-1676.
15. 15. Agalidis, I., Ivancich, A., Mattioli, T.A. & Reiss-Husson, F. (1997) Characterization of the Rhodocyclus tenuis photosynthetic reaction center. Biochim. Biophys. Ada 1321, 31-46.
16. 16. Fling, S.P. & Gregerson, D.S. (1986) Peptide and protein molecular weight determination by electrophoresis using a high molecularity Tris buffer system without urea. Anal. Biochem. 155, 83-88.
17. 17. Goodhew, C.F., Brown, K.R. & Pettigrew, G.W. (1986) Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes. Biochim. Biophys. Acta 852, 288-294.
18. 18. Bauw, G., Van Damme, J., Puype, M., Vandekerckhove, J., Gesser, B., Ratz, G.P., Laurissen, J., B. & Celis, J.E. (1989) Protein-electroblotting and -microsequencing strategies in generating protein data bases from two-dimensional gels. Proc. Natl Acad. Sci. USA 86, 7701-7705.
19. 19. Le Caer, J.P. & Rossier, J. (1988) On the use of polyethyleneimine as a carrier for protein sequencing. Comparison with polybrene. Anal. Biochem. 169, 246-252.
20. 20. Berry, E.A. & Trumpower, B.L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15.
21. 559 and iron protoporphyrin TX-bisimidazole model compounds. Biochemistry 31, 11460-11471.
22. 2. A resonance Raman study. Biochemistry 36, 5499-5508.
23. 23. Fukushima, A., Matsuura, K., Shimada, K. & Satoh, T. (1988) Reaction center-B870: pigment protein complexes with bound cytochromes c-555 and c-551 from Rhodocyclus gelatinosus. Biochim. Biophys. Acta 933, 399-405.
24. 24. Weyer, K.A., Schafer, W., Lottspeich, F. & Michel, H. (1987) The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein. Biochemistry 26, 2909-2291.
25. 2- Biochim. Biophys. Acta 809, 291-310.
26. 26. Kihara, T. & Mc Cray, J. (1973) Water and cytochrome oxidation-reduction reactions. Biochim. Biophys. Acta 292, 297-309.
27. 27. De Vries, S. & Albracht, S.P.J. (1979) Intensity of highly anisotropic low-spin heme EPR signals. Biochim. Biophys. Acta 546, 334-340.
28. 28. Othman, S., Le Lirzin, A. & Desbois, A. (1994) Resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: characterization of the bis[histidine] axial ligation in c-type cytochromes. Biochem. 33, 15437-15448.
29. 29. Othman, S. & Desbois, A. (1998) Resonance Raman investigation of lysine and N-acetylmethionine complexes of ferric and ferrous microperoxidase. Influences of the axial ligation on the heme c structure. Eur. Biophys. J. 28, 12-25.
30. 30. Desbois, A. (1994) Resonance Raman spectroscopy of c-type cytochromes. Biochimie 76, 693-707.
31. 31. Stallard, B.R., Callis, P.R., Champion, P. & Albrecht, A.C. (1984) Application of the transform theory to resonance Raman excitation profiles in the Soret region of cytochrome-c. J. Chem. Phys. 80, 70-82.
32. 32. Othman, S., Le Lirzin, A. & Desbois, A. (1993) A heme c-peptide model system for the resonance Raman study of c-type cytochromes: characterization of the solvent-dependence of peptide-histidine-heme interactions. Biochemistry 32, 9781-9791.
33. 33. Sieber, B. (1995) Elektrochemische und spektroskopische Untensuchungen den Tetrahëm-Cytochrom-untereinheit von Rubrivivax gelatinosus, Diplomearbeit, Freiburg University, Germany.
34. 34. Creutz, C. (1981) The complexities of ascorbate as a reducing agent. Inorg. Chem. 20, 4449-4452.
35. 8 depending on the ambient redox potential. Biochemistry 36, 12183-12188.
36. 36. Garcia, D., Richaud, P., Breton, J. & Verméglio, A. (1994) Structural function of the tetraheme cytochrome associated to the reaction center of Roseobacter denitrificans. Biochimie 76, 666-673.
37. 37. Dracheva, S.M., Drachev, L.A., Zaberezhnaya, S.M., Konstantinov, A.A., Semenov, A.Y. & Skulachev, V.P. (1986) Spectral, redox and kinetic characteristics of high-potential cytochrome hemes in Rhodopseudomonas viridis reaction center. FEBS Lett. 205, 41-46.
38. 38. Romberg, R.W. & Kassner, R.J. (1982) Effects of solvent on the absorption maxima of five-coordinate heme complexes and carbon monoxide-heme complexes as models for the differential spectral properties of hemoglobins and myoglobins. Biochemistry 21, 880-886.
39. 39. Champion, P.M., Collins, D.W. & Fitchen, D.B. (1976) Resonance Raman spectra of heme proteins at low temperature. J. Am. Chem. Soc. 98, 7114-7115.
40. 40. Adar, F. (1978) Electronic absorption spectra of hemes and hemoproteins. In: The Porphyrins (Dolphin, D., ed.), Vol. 3, pp. 167-209. Academic Press, New York.
41. 41. Meyer, T.E., Kennel, S.J., Tedro, S.M. & Kamen, M.D. (1973) Iron protein content of Thiocapsa pfennigii, a purple sulfur bacterium of atypical chlorophyll composition. Biochim. Biophys. Acta 292, 634-643.
42. 42. Doi, M., Takamya, K.I. & Nishimura, M. (1983) Isolation and properties of membrane-bound cytochrome c-552 from photosynthetic bacterium Chromatium vinosum. Photosynth. Res. 4, 49-60.
43. 43. Leguijt, T. & Hellingwerf, K.J. (1991) Characterization of reaction center/antenna complexes from bacteriochlorophyll-a containing Ectothiorhodospiraceae. Biochim. Biophys. Acta 1057, 353-360.
44. 44. Van Vliet, P., Zannoni, D., Nitschke, W. & Rutherford, A.W. (1991) Membrane-bound cytochromes in Chloroflexus aurantiacus studied by EPR. Ear. J. Biochem. 199, 317-323.
45. 45. Nitschke, W., Jubaultbregler, M. & Rutherford, A.W. (1993) The reaction center associated tetraheme cytochrome subunit from Chromatium-vinosum revisited - a reexamination of its EPR properties. Biochemistry 32, 8871-8879.
46. 553, Biochem. 36, 1927-1932.
47. 47. Heibel, G., Griebenow, K. & Hildebrandt, P. (1991) Structural studies of cytochrome c-554 from Chloroflexus aurantiacus by resonance Raman spectroscopic techniques. Biochim. Biophys. Acta 1060, 196-202.
48. 48. Nagashima, K.V.P., Shimada, K. & Matsuura, K. (1993) Phylogenetic analysis of photosynthetic genes of Rhodocyclus gelatinnsus: possibility of horizontal gene transfer in purple bacteria. Photosynth. Res. 36, 185-191.
49. 49. Moore, G.R. & Pettigrew, G.W. (1990) Redox potentials. In Cytochromes C: Evolutionary, Structural and Physicochemical Aspects, pp. 309-402. Springer, Berlin,
50. 6. The effects of axial ligand plane orientation on the EPR and Mossbauer spectra of low-spin ferrihemes. J. Am. Chem. Soc. 108, 5288-5297.
51. 51. Kassner, R.J. (1972) Effects of nonpolar environments on the redox potentials of heme complexes. Proc. Natl Acad. Sci. USA 69, 2263-2267.
52. 52. Stellwagen, E. (1978) Haem exposure as the determinate of oxidation-reduction potential of haem proteins. Nature 275, 73-74.
53. 53. Kennel, S.J. & Kamen, M.D. (1971) Iron-containing proteins in Chromatium. II. Purification and properties of cholate-solubilized cytochrome complex. Biochim. Biophys. Acta 253, 153-166.
54. 54. Freeman, J.C. & Blankenship, R.E. (1990) Isolation and characterization of the membrane-bound cytochrome c-554 from the thermophilic green photosynthetic bacterium Chloroflexus aurantiacus. Photosynth. Res. 23, 29-38.
55. 55. Nagashima, K.V.P., Sakuragi, Y., Shimada, K. & Matsuura, K. (1998) Comparative analysis of the primary structure of the reaction center-bound cytochrome subunil in purple bacteria. Photosynth. Res. 55, 349-355.