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Errors in the studies of enzymatic reactions resulting from unforeseen oxidation-reduction reactions
Języki publikacji
Abstrakty
Reakcje enzymatyczne są najczęściej monitorowane za pomocą pomiarów spektrofotometrycznych przy jednej długości fali. Jest to zwykle bezpieczne, gdy stosuje się tylko standardowy substrat dający znany produkt. Jeśli jednak bada się mieszaninę związków, np. substratu i potencjalnych inhibitorów, to mogą pojawić się poważne błędy. Często zachodzą bowiem wówczas niespodziewane reakcje. Potencjalne inhibitory same mogą być substratami enzymu, albo mogą reagować z produktem lub intermediatami przekształcania substratu. Spodziewany produkt może więc nie powstać, albo powstają produkty uboczne z widmami absorpcji zupełnie różnymi od oczekiwanego produktu lub też nakładającymi się na to widmo, co daje kompletnie fałszywe wyniki.
Enzymatic reactions are usually monitored using spectrophotometric measurements at one wavelength. Such measurements usually pose no risk, if a standard substrate that gives known product is used. However, if a mixture of compounds is studied, e.g. a substrate and potential inhibitors, this may lead to serious errors. In such cases unexpected reactions often occur. The potential inhibitors might be themselves enzyme substrates or might react with the product or intermediates of substrate conversion. Therefore, the expected product might not be produced or by-products are formed with spectra completely differently from the expected product or overlapping with this spectrum what might give totally false results.
Czasopismo
Rocznik
Tom
Strony
341--346
Opis fizyczny
Bibliogr. 22 poz., rys.
Twórcy
autor
- Wydział Chemii, Uniwersytet Opolski, Opole
autor
- Wydział Chemii, Uniwersytet Opolski, Opole
Bibliografia
- 1. Sanchez-Ferrer, A., Rodriguez-Lopez, J. N., Garcia-Canovas, F., Garcia-Carmona, F.: Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1995, 1247, 1–11.
- 2. Lejczak, B., Kafarski, P., Makowiecka, E.: Phosphonic analogues of tyrosine and 3,4-dihydroxyphenylalanine (dopa) influence mushroom tyrosinase activity. Biochem. J. 1987, 242, 81–88.
- 3. Gasowska, B., Wojtasek, H., Hurek, J., Drag, M., Nowak, K., Kafarski, P. Redox reaction between amino-(3,4-dihydroxyphenyl)methyl phosphonic acid and dopaquinone is responsible for the apparent inhibitory effect on tyrosinase. Eur. J. Biochem. 2002, 269, 4098–104.
- 4. Reszka, K. J., Britigan, B. E.: Doxorubicin inhibits oxidation of 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) by a lactoperoxidase/H2O2 system by reactingwith ABTS-derived radical. Arch. Biochem. Biophys. 2007, 466, 164–71.
- 5. Re, R., Pellegrini, N., Proteggente, A., Pannala, A., Yang, M., Rice-Evans, C. Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic. Biol. Med. 1999, 26, 1231–7.
- 6. Bartosz, G.: Non-enzymatic antioxidant capacity assays: Limitations of use in biomedicine. Free Radic. Res. 2010, 44, 711–20.
- 7. Wood, J. M., Chavan, B., Hafeez, I., Schallreuter, K. U.: Regulation of tyrosinase by tetrahydropteridines and H2O2. Biochem. Biophys. Res. Commun. 2004, 325, 1412–7.
- 8. Jung, J. H., Choi, S. W., Han, S.: Indirect oxidation of 6-tetrahydrobiopterin by tyrosinase. Biochem. Biophys. Res. Commun. 2004, 314, 937–42.
- 9. Wojtasek, H.: Regulation of tyrosinase by tetrahydropteridines--what is real? A comment on the work published by Wood et al. on December 24, 2004. Biochem. Biophys. Res. Commun. 2005, 329, 801–3.
- 10. Wood, J. M., Chavan, B., Hafeez, I., Schallreuter, K. U.: Regulation of tyrosinase by tetrahydropteridines--what is real? A critical reanalysis of H. Wojtasek’s view. Biochem. Biophys. Res. Commun. 2005, 331, 891–3.
- 11. Pomerantz, S. H.: The tyrosine hydroxylase activity of mammalian tyrosinase. J. Biol. Chem. 1966, 241, 161–8.
- 12. Müller, G. H., Waldmann, H.: The phenyl hydrazide as an enzyme-labile protecting group – oxidative cleavage with mushroom tyrosinase. Tetrahedron Lett. 1999, 40, 3549–4552.
- 13. Volkert, M., Koul, S., Müller, G. H., Lehnig, M., Waldmann, H.: Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis. J. Org. Chem. 2002, 67, 6902–10.
- 14. Gasowska, B., Frackowiak, B., Wojtasek, H.: Indirect oxidation of amino acid phenylhydrazides by mushroom tyrosinase. Biochim. Biophys. Acta 2006, 1760, 1373–9.
- 15. Wang, J., Chen, L.: Hydrazine detection using a tyrosinase-based inhibition biosensor. Anal. Chem. 1995, 67, 3824–3827.
- 16. Espin, J. C., Jolivet, S., Wichers, H. J.: Inhibition of mushroom polyphenol oxidase by agaritine. J. Agric. Food Chem. 1998, 46, 2976–2980.
- 17. Espin, J. C., Jolivet, S., Overeem, A., Wichers, H. J.: Agaritine from Agaricus bisporus is capable of preventing melanin formation. Phytochemistry 1999, 50, 555–563.
- 18. Patel, R. P., Okun, M. R.: Hydroxylation of tyrosine by plant peroxidase and mushroom tyrosinase, with and without hydrazine, to retard the oxidation of dopa. Physiol. Chem. Phys. 1977, 9, 85–9.
- 19. Riley, P. A.: Melanogenesis and melanoma. Pigment Cell Res. 2003, 16, 548–52.
- 20. Gasowska-Bajger, B., Frackowiak-Wojtasek, B., Koj, S., Cichon, T., Smolarczyk, R., Szala, S., Wojtasek, H.: Oxidation of carbidopa by tyrosinase and its effect on murine melanoma. Bioorg. Med. Chem. Lett. 2009, 19, 3507–10.
- 21. Frackowiak-Wojtasek, B., Gasowska-Bajger, B., Mazurek, M., Raniszewska, A., Logghe, M., Smolarczyk, R., Cichon, T., Szala, S., Wojtasek, H.: Synthesis and analysis of activity of a potential anti-melanoma prodrug with a hydrazine linker. Eur. J. Med. Chem. 2014, 71, 98–104.
- 22. Kucukguzel, S. G., Kucukguzel, I., Ulgen, M.: Metabolic and chemical studies on N-(4-chlorobenzyl)-N’-benzoylhydrazine. Il Farmaco 2000, 55, 624–30.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-c36b499a-d324-4cf1-a38d-cb0e0b9e04c0