Resonance Raman study of multihemic c-type cytochromes from Desulfuromonas acetoxidans

European Journal of Biochemistry

Volumn 267, Issue 4, 2000, Pages 1050-1058

  Chottard, Geneviève ^a   Kazanskaya, Irina ^a   Bruschi, Mireille ^b  

^a SORBONNE UNIVERSITÉ   (France)

^b CNRS   (France)

Author keywords

CD; Fe His vibration; Multihemic c type cytochrome; RR spectra; Spectroelectrochemistry

Indexed keywords

CYTOCHROME C OXIDASE; HEME;

ARTICLE; DESULFOVIBRIO; ELECTROCHEMISTRY; ENZYME ASSAY; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; RAMAN SPECTROMETRY; SULFATE REDUCING BACTERIUM; VIBRATION;

ASCORBIC ACID; CIRCULAR DICHROISM; CYTOCHROME C GROUP; DELTAPROTEOBACTERIA; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HEME; HISTIDINE; HYDROGEN-ION CONCENTRATION; LIGANDS; MOLECULAR WEIGHT; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN; SULFUR-REDUCING BACTERIA; TITRIMETRY;

BACTERIA (MICROORGANISMS); DESULFOVIBRIO; DESULFUROMONAS ACETOXIDANS;

EID: 0033977885     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01096.x     Document Type: Article

References (41)

1. 1. Ambler, R.P. (1991) Sequence variability in bacterial cytochromes c. Biochim. Biophys. Acta 1058, 42-47.
2. 3. J. Biol. Chem. 257, 14341-14348.
3. 3 from Desulfovibrio desulfuricans Norway at 1.7 Å resolution. J. Mol. Biol. 243, 653-667.
4. 4. Morais, J., Nuno Palma, P., Frazao, C., Caldeira, J., Le Gall, J., Moura, I., Moura, J.J.G. & Carrondo, M.A. (1995) Structure of the tetraheme cytochrome from Desulfovibrio desulfuricans ATCC 27774: X-ray diffraction and electron paramagnetic resonance studies. Biochemistry 34, 12830-12841.
5. 3 at 1.8 Å resolution. J. Mol. Biol. 172, 109-139.
6. 3 from Desulfovibrio vulgaris Hildenborough at 2 Å resolution. J. Biochem. 110, 532-540.
7. 3 from Desulfovibrio vulgaris Hildenborough at 1.9 Å resolution. J. Mol. Biol. 234, 680-699.
8. 3 from Desulfovibrio gigas: crystal structure at 1.8 Å resolution and evidence for a specific calcium-binding site. Protein Sci. 5, 1342-1354.
9. 3 (Mr 26000) isolated from sulfate-reducing bacteria and its relationships to other polyhemic cytochromes from Desulfovibrio. Methods Enzymol. 243, 140-155.
10. r 26000) from Desulfovibrio desulfuricans Norway. Structure 4, 395-404.
11. 3 from Desulfovibrio gigas containing disulfide bridges. J. Biol. Inorg. Chem. 4, 162-165.
12. 12. Higuchi, Y., Yagi, T. & Voordouw, G. (1994) Hexadecaheme cytochrome c. Methods Enzymol. 243, 155-165.
13. 13. Matias, P.M., Coelho, R., Pereira, I.A.C., Coelho, A.V., Thompson, A.W.R., Sieker, L.C., Le Gall, J. & Carrondo, M.A. (1999) The primary and three dimensional structures of a nine-heme cytochrome c from Desulfovibrio desulfuricans ATCC27774 reveal a new member of the Hmc family. Structure 7, 119-130.
14. 7) from Desulfuromonas acetoxidans. Biochim. Biophys. Acta 460, 58-64.
15. 15. Bruschi, M., Woudstra, M., Guigliarelli, B., Asso, M., Lojou, E., Pétillot Y. & Abergel, C. (1997) Biochemical and spectroscopic characterization of two new cytochromes isolated from Desulfuromonas acetoxidans. Biochemistry 36, 10601-10608.
16. 16. Pereira, I.A.C., Pacheco, I., Liu, M.Y., Le Gall, J., Xavier, A.V. & Teixeira, M. (1997) Multiheme cytochromes from the sulfur-reducing bacterium Desulfuromonas acetoxidans. Eur. J. Biochem. 248, 323-328.
17. 7). Eur. J. Biochem. 144, 433-440.
18. 551.5 from Desulfuromonas acetoxidans. Biochim. Biophys. Acta 579, 269-278.
19. 1H NMR. J. Biol. Inorg. Chem. 1, 305-311.
20. 3 from Desulfuromonas acetoxidans. Eur. J. Biochem. 243, 474-481.
21. 7 from. Desulfuromonas acetoxidans. Proc. Natl Acad. Sci. USA 93, 14396-14400.
22. 7 from Desulfuromonas acetoxidans. Eur. J. Biochem. 256, 261-270.
23. 3: spectroelectrochemical evidence for a conformational change triggered by heme IV reduction. Biochemistry 35, 13411-13418.
24. 24. Desbois, A. (1994) Resonance Raman spectroscopy of c-type cytochromes. Biochimie 76, 693-707.
25. 3. Biochemistry 37, 12431-12442.
26. 26. Othman, S., Le Lirzin, A. & Desbois, A. (1994) Resonance Raman investigation of imidazole and imidazolate complexes of micro-peroxidase: characterization of the bis (histidine) axial ligation in c-type cytochromes. Biochemistry 33, 15437-15448.
27. 27. Hu, S., Morris, Y.K., Singh, J.P., Smith, K.M. & Spiro, T.G. (1993) Complete assignment of cytochrome c resonance Raman spectra via enzymatic reconstitution with isotopically labeled hemes. J. Am. Chem. Soc. 115, 12446-12458.
28. th International Conference on Raman Spectroscopy (Clark, R.J.H. & Long, D.A., eds), pp. 677-678. Wiley, Chichester, UK.
29. 29. Desbois, A. & Lutz, M. (1981) Low-frequency vibrations of ferroporphyrin-substituted imidazole complexes. A resonance Raman study. Biochim. Biophys. Acta 671, 168-176.
30. 2H isiotope shifts and normal coordinate calculations. J. Phys. Chem. 91, 4690-4696.
31. 31. Desbois, A. & Lutz, M. (1992) Redox control of proton transfers in membrane b-type cytochromes: an absorption and resonance Raman study on bis (imidazole) and bis (imidazolate) model complexes of iron-protoporphyrin. Eur. Biophys. J. 20, 321-335.
32. 32. Li, X.-Y. & Spiro, T.G. (1988) Is bound CO linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data. J. Am. Chem. Soc. 110, 6024-6033.
33. 1H-NMR. FEBS Lett. 390, 59-62.
34. 3 from Desulfovibrio desulfuricans Norway strain. J. Mol. Biol. 216, 161-166.
35. 1H nuclear magnetic resonance spectroscopy. Biochem. J. 294, 899-908.
36. 3 by 2D-NMR. FEBS Lett. 314, 155-158.
37. 37. Park, J.S., Ohmura, T., Kano, K., Sagara, T., Niki, K., Kyogoku, Y. & Akutsu, H. (1996) Regulation of the redox order of four hemes by pH in cytochrome c from D. vulgaris Miyazaki F. Biochim. Biophys. Acta 1293, 45-54.
38. 1H nuclear magnetic resonance spectroscopy. Biochem. J. 294, 909-915.
39. 3 from Desulfovibrio vulgaris. Eur. J. Biochem. 241, 723-731.
40. 3 from several Desulfovibrio species using continuum electrostatic methods. J. Biol. Inorg. Chem. 4, 73-86.
41. 41. Brugna, M., Nitschke, W., Toci, R., Bruschi, M. & Giudici-Orticoni, M.T. (1999) First evidence for the presence of a hydrogenase in the sulfur-reducing bacterium Desulfuromonas acetoxidans. J. Bacteriol. 181, 5505-5508.