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Hemoglobin, horseradish peroxidase, and heme-bovine serum albumin as biocatalyst for the oxidation of dibenzothiophene

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Abstract

Hemoglobin, horseradish peroxidase, and bovine serum albumin incubated heme-catalyzed the oxidation of dibenzothiophene into sulfoxide in the presence of hydrogen peroxide. This reaction was carried out in an aqueous buffer containing 25% of water-miscible organic solvents. The observation of this transient state of hemoproteins during sulfoxidation showed heme degradation. None of the compounds usually involved in a classical peroxidative activity mechanism were detected. Furthermore, this activity did not appear to be based on a Fenton-type reaction. The highest degrees of sulfoxidation were obtained with hemoglobin. Under the best conditions of reaction, 100% of dibenzothiophene were converted into dibenzothiophene sulfoxide by hemoglobin. Heat-denatured hemoproteins did keep their sulfoxidation activity. With hemoglobin, a kcat of 0.22 min-1 was determined. Nearly the same values were obtained with heat-denatured hemoglobin and bovine serum albumin-adsorbed heme. With horseradish peroxidase, only 4% of conversion was attained. This percentage could be slightly increased by using a less pure peroxidase or heat-denatured peroxidase.

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Abbreviations

Heme:

iron protoporphyrin IX regardless of the oxidation and ligation state

Hb:

hemoglobin

HRP:

horseradish peroxidase

DBT:

dibenzothiophene

SOD:

Superoxide dismutase

BSA:

bovine serum albumin

ABTS:

2,2−azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)

SDS-PAGE:

sodium dodecyl sulfate-polyacrylamide gel electrophoresis

DMF:

N,N-dimethylformamide

Hemin:

chloroprotoporphyrin IX iron (III)

HPLC:

high-pressure liquid chromatography

GC/MS:

gas chromatography/mass spectroscopy

DMSO:

dimethylsulfoxide

EDTA:

ethylenediaminetetraacetic acid

DTPA:

diethylenetriaminepentaacetic acid

References

  1. Wariishi, H., Valli, K., and Renganathan, V. (1989),J. Biol. Chem. 264, 14,185–14,191.

    CAS  Google Scholar 

  2. Juliette, L. Y., Hyman, M. R., and Arp, D. J. (1993),Appl. Environ. Microbiol. 59, 3718–3727.

    CAS  Google Scholar 

  3. Piette, L. H., Bulow, G., and Yamazaki, I. (1964),Biochim. Biophys. Acta 88, 120–129.

    CAS  Google Scholar 

  4. Kobayashi, S., Nakano, S., Goto, T., Kimura, T., and Schaap, A. P. (1986),Biochem. Biophys. Res. Commun. 135, 166–171.

    Article  CAS  Google Scholar 

  5. Doerge, D. (1986),Arch. Biochem. Biophys. 244, 678–685.

    Article  CAS  Google Scholar 

  6. Colonna, S., Gaggero, N., Manfredi, A., Casella, L., Gullotti, M., Carrea, G., and Pasta, P. (1990),Biochemistry 29, 10,465–10,468.

    Article  CAS  Google Scholar 

  7. Casella, L., Gullotti, M., Ghezzi, R., Poli, S., Beringhelli, T., Colonna, S., and Carrea, G. (1992),Biochemistry 31, 9451–9459.

    Article  CAS  Google Scholar 

  8. Klyachko, N. L. and Klibanov, A. M. (1992),Appl. Biochem. Biotechnol. 37, 53–68.

    CAS  Google Scholar 

  9. Dunford, H. B. (1991), inPeroxidases in Chemistry and Biology, vol. 2, Everse, J., Everse, K. E., and Grisham, M. B., eds., CRC, Boca Raton, pp. 1–24.

    Google Scholar 

  10. Keilin, D. and Hartree, E. F. (1950),Nature 166, 513–514.

    Article  CAS  Google Scholar 

  11. King, N. K. and Winfield, M. E. (1963),J. Biol. Chem. 238, 1520–1528.

    CAS  Google Scholar 

  12. Ohlsson, P. I., and Paul, K. G. (1976),Acta Chem. Scand. B30, 373–375.

    Article  CAS  Google Scholar 

  13. Kelder, P. P., de Mol, N. J., and Janssen, L. H. L. (1989),Biochem. Pharmacol. 38, 3593–3599.

    Article  CAS  Google Scholar 

  14. Nelson, D. P. and Kiesow, L. A. (1972),Anal. Biochem. 49, 474–478.

    Article  CAS  Google Scholar 

  15. Faison, B. D., Clark, T. M., Lewis, S. N., Ma, C. Y., Sharkey, D. M., and Woodward, C. A. (1991),Appl. Biochem. Biotechnol. 28/29, 237–251.

    Google Scholar 

  16. Rachmilewitz, E. A., Peisach, J., and Blumberg, W. E. (1971),J. Biol. Chem. 246, 3356–3366.

    CAS  Google Scholar 

  17. Giulivi, C. and Cadenas, E. (1993),FEBS 332, 287–290.

    Article  CAS  Google Scholar 

  18. Perez, U. and Dunford, H. B. (1990),Biochim. Biophys. Acta 1038, 98–104.

    CAS  Google Scholar 

  19. Gutteridge, J. M. C., Richmond, R., and Halliwell, B. (1979),Biochem. J. 184, 469–472.

    CAS  Google Scholar 

  20. Gutteridge, J. M. C. (1986),FEBS Lett. 201, 291–295.

    Article  CAS  Google Scholar 

  21. Puppo, A. and Halliwell, B. (1988),Biochem. J. 249, 185–190.

    CAS  Google Scholar 

  22. Arnao, M. B., Acosta, M., Del Rio, J. A., Varón, R., and Garcia-Cánovas, F. (1990),Biochim. Biophys. Acta 1041, 43–47.

    CAS  Google Scholar 

  23. Vincent, S. H., Grady, R. W., Shaklai, N., Snider, J. M., and Muller-Eberhard, U. (1988),Arch. Biochem. Biophys. 265, 539–550.

    Article  CAS  Google Scholar 

  24. Beaven, G. H., d’Albis, A., and Gratzer, W. B. (1974),Eur. J. Biochem. 41, 539–546.

    Article  CAS  Google Scholar 

  25. Shin, W. S., Yamashita, H., and Hirose, M. (1994),Biochem. J. 304, 81–86.

    CAS  Google Scholar 

  26. Rice, R. H., Lee, Y. M., and Brown, W. D. (1983),Arch. Biochem. Biophys. 221, 417–427.

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Laboratoire de Technologie Enzymatique, Unité de recherche associée 1442 du Centre National de La Recherche Scientifique, Université de Technologie de Compiegne, BP 649-60206, Compiegne Cédex, France

    Thérèse Stachyra, Sylviane Pulvin & Daniel Thomas

  2. Laboratoire de Technologie des Substances Naturelles, Villeneuve d’Ascq Cédex, France

    Didier Guillochom

Authors
  1. Thérèse Stachyra
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  2. Didier Guillochom
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  3. Sylviane Pulvin
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  4. Daniel Thomas
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Stachyra, T., Guillochom, D., Pulvin, S. et al. Hemoglobin, horseradish peroxidase, and heme-bovine serum albumin as biocatalyst for the oxidation of dibenzothiophene. Appl Biochem Biotechnol 59, 231–243 (1996). https://doi.org/10.1007/BF02783567

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  • DOI: https://doi.org/10.1007/BF02783567

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