Calcium-dependent heme structure in the reduced forms of the bacterial cytochrome c peroxidase from Paracoccus pantotrophus

Biochemistry

Volumn 47, Issue 21, 2008, Pages 5841-5850

  Pauleta, Sofia R ^a,b   Lu, Yi ^b,c   Goodhew, Celia F ^d   Moura, Isabel ^a   Pettigrew, Graham W ^d   Shelnutt, John A ^a,b,c  

^a UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^b SANDIA NATIONAL LABORATORIES   (United States)

^c UNIVERSITY OF GEORGIA   (United States)

^d UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS; RAMAN SCATTERING; REDUCTION; RESONANCE;

FERRIC PEROXIDATIC HEME; PARACOCCUS PANTOTROPHUS;

BACTERIA;

CALCIUM; CYTOCHROME C PEROXIDASE; HEME;

ARTICLE; BINDING SITE; CALCIUM BINDING; ENZYME ACTIVITY; ENZYME METABOLISM; NONHUMAN; PARACOCCUS PANTOTROPHUS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; RAMAN SPECTROMETRY;

BIOCHEMISTRY; CALCIUM; CATIONS; CYTOCHROME-C PEROXIDASE; ENZYME ACTIVATION; HEME; IONS; MAGNESIUM; MODELS, CHEMICAL; MOLECULAR CONFORMATION; OXYGEN; PARACOCCUS PANTOTROPHUS; PROTEIN CONFORMATION; SPECTRUM ANALYSIS, RAMAN;

BACTERIA (MICROORGANISMS); PARACOCCUS PANTOTROPHUS;

EID: 44349131080     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702486d     Document Type: Article

References (34)

1. Lesser, M. P. (2006) Oxidative stress in marine environments: Biochemistry and physiological ecology. Annu. Rev. Physiol. 68, 253-278.
2. Soininen, R., and Ellfolk, N. (1972) Pseudomonas cytochrome c peroxidase. 4. Some kinetic properties of peroxidation reaction, and enzymatic determination of extinction coefficients of Pseudomonas cytochrome c-551 and azurin. Acta Chem. Scand. 26, 861-872.
3. Pauleta, S. R., Guerlesquin, F., Goodhew, C. F., Devreese, B., Van Beeumen, J., Pereira, A. S., Moura, I., and Pettigrew, G. W. (2004) Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase. Biochemistry 43, 11214-11225.
4. Ronnberg, M., and Ellfolk, N. (1979) Heme-linked properties of Pseudomonas cytochrome c peroxidase: Evidence for non-equivalence of the hemes. Biochim. Biophys. Acta 581, 325-333.
5. Hanlon, S. P., Holt, R. A., and Mcewan, A. G. (1992) The 44 kDa c-type cytochrome induced in Rhodobacter capsulatus during growth with dimethylsulfoxide as an electron-acceptor is a cytochrome-c peroxidase. FEMS Microbiol. Lett. 97, 283-288.
6. Hu, W., De Smet, L., Van Driessche, G., Bartsch, R. G., Meyer, T. E., Cusanovich, M. A., and Van Beeumen, J. (1998) Characterization of cytochrome c-556 from the purple phototrophic bacterium Rhodobacter capsulatus as a cytochrome c peroxidase. Eur. J. Biochem. 258, 29-36.
7. Arciero, D. M., and Hooper, A. B. (1994) A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states. J. Biol. Chem. 269, 11878-11886.
8. Alves, T., Besson, S., Duarte, L. C., Pettigrew, G. W., Girio, F. M. F., Devreese, B., Vandenberghe, I., Van Beeumen, J., Fauque, G., and Moura, I. (1999) A cytochrome c peroxidase from Pseudomonas nautica 617 active at high ionic strength: Expression, purification and characterization. Biochim. Biophys. Acta 1434, 248-259.
9. 2+ and the bacterial peroxidases: The cytochrome c peroxidase from Pseudomonas stutzeri. J. Biol. Inorg. Chem. 8, 29-37.
10. Zahn, J. A., Arciero, D. M., Hooper, A. B., Coats, J. R., and DiSpirito, A. A. (1997) Cytochrome c peroxidase from Methylococcus capsulatus Bath. Arch. Microbiol. 168, 362-372.
11. Goodhew, C. F., Wilson, I. B. H., Hunter, D. J. B., and Pettigrew, G. W. (1990) The cellular location and specificity of bacterial cytochrome c peroxidases. Biochem. J. 271, 707-712.
12. Echalier, A., Goodhew, C. F., Pettigrew, G. W., and Fulop, V. (2006) Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus. Structure 14, 107-117.
13. Gilmour, R., Goodhew, C. F., Pettigrew, G. W., Prazeres, S., Moura, I., and Moura, J. J. G. (1993) Spectroscopic characterization of cytochrome c peroxidase from Paracoccus denitrificans. Biochem. J. 294, 745-752.
14. Pauleta, S. R., Lu, Y., Goodhew, C. F., Moura, I., Pettigrew, G. W., and Shelnutt, J. A. (2001) Calcium-dependent conformation of a heme and fingerprint peptide of the diheme cytochrome c peroxidase from Paracoccus pantotrophus. Biochemistry 40, 6570-6579.
15. Pettigrew, G. W., Goodhew, C. F., Cooper, A., Nutley, M., Jumel, K., and Harding, S. E. (2003) The electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans. Biochemistry 42, 2046-2055.
16. Yamamoto, T., Palmer, G., FGill, D., Salmeen, I. T., and Lajos, R. (1973) The valence and spin state of iron in oxyhemoglobin as inferred from resonance Raman spectroscopy. J. Biol. Chem. 248, 5211-5213.
17. Spiro, T. G., and Strekas, T. C. (1974) Resonance Raman spectra of heme proteins. Effects of oxidation and spin state. J. Am. Chem. Soc. 96, 338-345.
18. Spiro, T. G., and Burke, J. M. (1976) Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues. J. Am. Chem. Soc. 98, 5482-5489.
19. Spiro, T. G. (1982) in Iron Porphyrins (Lever, A. B. P., and Gray, H. B., Eds.) pp 89, Addison-Wesley, Reading, MA.
20. Alden, R. G., Crawford, B. A., Doolen, R., Ondrias, M. R., and Shelnutt, J. A. (1989) Ruffling of nickel(II) octaethylporphyrin in solution. J. Am. Chem. Soc. 111, 2070-2072.
21. Li, X. Y., Czernuszewicz, R. S., Kincaid, J. R., and Spiro, T. G. (1989) Consistent porphyrin force-field. 3. Out-of-plane modes in the resonance Raman-spectra of planar and ruffled nickel octaethylporphyrin. J. Am. Chem. Soc. 111, 7012-7023.
22. Shelnutt, J. A., Medforth, C. J., Berber, M. D., Barkigia, K. M., and Smith, K. M. (1991) Relationships between structural parameters and Raman frequencies for some planar and nonplanar nickel(II) porphyrins. J. Am. Chem. Soc. 113, 4077-4087.
23. Shelnutt, J. A., Majumder, S. A., Sparks, L. D., Hobbs, J. D., Medforth, C. J., Senge, M. O., Smith, K. M., Miura, M., Luo, L., and Quirke, J. M. E. (1992) Resonance Raman spectroscopy of nonplanar nickel porphyrins. J. Raman Spectrosc. 23, 523-529.
24. Song, X. Z., Jentzen, W., Jaquinod, L., Khoury, R. G., Medforth, C. J., Jia, S. L., Ma, J. G., Smith, K. M., and Shelnutt, J. A. (1998) Substituent-induced perturbation symmetries and distortions of meso-tert-butylporphyrins. Inorg. Chem. 37, 2117-2128.
25. Jentzen, W., Simpson, M. C., Hobbs, J. D., Song, X., Ema, T., Nelson, N. Y., Medforth, C. J., Smith, K. M., Veyrat, M., Mazzanti, M., Ramasseul, R., Marchon, J. C., Takeuchi, T., Goddard, W. A., and Shelnutt, J. A. (1995) Ruffling in a series of nickel(II) mesotetrasubstituted porphyrins as a model for the conserved ruffling of the heme of cytochromes c. J. Am. Chem. Soc. 117, 11085-11097.
26. Shelnutt, J. A., Song, X. Z., Ma, J. G., Jia, S. L., Jentzen, W., and Medforth, C. J. (1998) Nonplanar porphyrins and their significance in proteins. Chem. Soc. Rev. 27, 31-41.
27. 3. Biochemistry 37, 12431-12442.
28. Howes, B. D., Schiodt, C. B., Welinder, K. G., Marzocchi, M. P., Ma, J. G., Zhang, J., Shelnutt, J. A., and Smulevich, G. (1999) The quantum mixed-spin heme stale of barley peroxidase: A paradigm for class III peroxidases. Biophys. J. 77, 478-492.
29. Hu, S. Z., Morris, I. K., Singh, J. P., Smith, K. M., and 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.
30. Dasgupta, S., Rousseau, D. L., Anni, H., and Yonetani, T. (1989) Structural characterization of cytochrome c peroxidase by resonance Raman scattering. J. Biol. Chem. 264, 654-662.
31. 2+ binding sites of cytochrome c peroxidase from Paracoccus denitrificans. Eur. J. Biochem. 234, 878-886.
32. Pettigrew, G. W., Echalier, A., and Pauleta, S. R. (2006) Structure and mechanism in the bacterial dihaem cytochrome c peroxidases. J. Inorg. Biochem. 100, 551-567.
33. Franco, R., Ma, J. G., Lu, Y., Ferreira, G. C., and Shelnutt, J. A. (2000) Porphyrin interactions with wild-type and mutant mouse ferrochelatase. Biochemistry 39, 2517-2529.
34. Balny, C., Anni, H., and Yonetani, T. (1987) A stopped-flow study of the reaction of cytochrome c peroxidase with hydroperoxides. FEBS Lett. 221, 349-354.