Advertisement

The Optical Biosensor Study of Protein-Protein Interactions within Cytochromes P450 Containing Monooxygenase Systems

  • Alexander I. Archakov
  • Yuri D. Ivanov
Part of the Electronics and Biotechnology Advanced (EL.B.A.) Forum Series book series (ELBA, volume 3)

Abstract

The cytochromes P450 — containing liver microsomal monooxyganase systems play an important role in the oxidation of drugs, toxins, carcinogens, mutagens and other xenobiotics (Archakov and Bachmanova, 1990). It is known that microsomal cytochromes P450 (P450), in particular P450 2B4 (2B4), function by interacting with their redox partners — NADPH-cytochrome P450 reductase (Fp) and cytochrome b5 (b5). Mitochondrial cytochromes P450 (particularly P450scc) hydroxylate cholesterol by acquiring electrons from adrenodoxin (Ad), which in turn accepts them from adrenodoxin reductase (AdR). Similar mechanism operates in the case of bacterial P450s (for example, P450cam), whose electron donor is putidoredoxin (Pd), which acquires electrons from putidoredoxin reductase (PdR). In some studies, protein-protein interactions were explored by the the spin equilibrium shift (Backes et al., 1985; Tamburini et al., 1985; Lapko et al., 1991; Gerber and Sligar, 1994) and the fluorescence quenching techniques (Davydov et al., 1996), based on which the affinities and kinetic constants of P450 complexes were determined. In other studies, kinetic electron transfer rate constants for interprotein electron transfer were reported (Cush et al., 1993; Tamburini et al., 1985; Eyer and Backes, 1992; Kanaeva et al., 1992; Wu et al., 1994; Voznesensky and Shenkman, 1992; Sevrukova et al., 1994; Gerber and Sligar, 1994; Lambeth and Kriengsiri, 1985; Lambeth and Kamin 1977; Nakamura et al., 1994). In present-day molecular interaction researches the ever-widening application is finding the optical biosensor method. It enables to study molecular interactions without protein labeling in real time (Johnsson et al., 1991; Cush et al., 1993; Davies et al., 1994; Yeung et al., 1995).

Keywords

Complex Formation Incubation Mixture Dissociation Rate Constant Redox Partner Binding Curve 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Archakov, A.I., and Bachmanova, G.I., 1990, Cytochrome P450 and Active Oxygen, Taylor & Francis, London, New York, Philadelphia.Google Scholar
  2. Bachmanova, G.I., Kanaeva, I.P., Stepanova, N.V., Koen, Y.M., Samenkova, N.F., and Archakov, A.I., 1995, Role of cytochrome b5 in microsomal soluble reconstituted monooxygenase system, in: Abstracts of 9thlnternational Conference on “Cytochrome P450. Biochemistry, Biophysics and Molecular Biology”, Zurich, Switzerland, 232.Google Scholar
  3. Backes, W.L., Tamburini, P.P., Jansson, I.J., Gibson, G.G., Sligar, S.G., and Schenkman, J.B., 1985, Kinetics of cytochrome P- 450 reduction: evidence for faster reduction of the high-spin ferric state, Biochemistry 24: 5130.CrossRefGoogle Scholar
  4. Chu, J.-W., and Kimura, T., 1973, Studies on adrenal steroid hydroxylases: molecular and catalytic properties of adrenodoxin reductase (a flavoprotein), J. Biol. Chem. 248: 2089.Google Scholar
  5. Cush, R., Gronin, J.M., Stewart, W.J., Maule, C.H., Molloy J., and Goddard, N.J., 1993, The resonant mirror: a novel optical biosensors for direct sensing of biomolecular interactions.Part I: Principle of operation and associated instrumentation, Biosensor and Bioelectronics 8: 347.CrossRefGoogle Scholar
  6. Davies, R.J., Edwards, P.R., Watts, H., Lowe, C.R., Buckle, P.E., Yeng, D., Kinning, T.M., and Pollard-Knight, D.V., 1994, The resonant mirror:a versatile tool for the study of biomolecular interactions, in: Techniques in Protein Chemistryt, Acad. Press Inc. 285.Google Scholar
  7. Davydov, D.R., Deprez, E., Hui Bon Hoa, G., Knushko, T.V., Kuznetsova, G.P., Koen, Y.M., and Archakov, A.I., 1995, High-pressure-induced transitions in microsomal cytochrome P450 2B4 in solution: evidence for conformational inhomogeneity in the oligomer, Arch.Biochem. Biophys. 320: 330.CrossRefGoogle Scholar
  8. Davydov, D., Knushko, T., Kanaeva, I., Koen, Y., Samenkova, N.F., Archakov, A., and Hui Bon Hoa, G., 1996, Interactions of cytochrome P4502B4 with NADPH-cytochrome P450 reductase studied by fluorescent probe, Biochimie 78: 734.CrossRefGoogle Scholar
  9. Eyer, C.S., and Backes, W.L., 1992, Relationship between the rate reductase-cytochrome P450 complex formation and the rate of first electrone transfer, Arch. Biochem. Biophys. 293: 231.CrossRefGoogle Scholar
  10. French, J.S., and Coon, M.G., 1979, Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes, Arch. Biochem.Biophys. 195: 565.CrossRefGoogle Scholar
  11. Gerber, N.C., and Sligar, S.G., 1994, A role for Asp-251 in cytochrome P450cam oxygen activation, J. Biol. Chem. 269: 4260.Google Scholar
  12. Gunsalus, I.C., and Wagner, G.C., 1978, Bacterial P450cam methylene monooxygenase components:cytochrome m, putidaredoxin, and putidaredoxin reductase, Methods Enzymol. 52: 166.CrossRefGoogle Scholar
  13. Janin, J., 1995, Principles of protein-protein recognition from structure to thermodynamics, Biochimie 77: 497.CrossRefGoogle Scholar
  14. Jonsson, U., Fagerstam, L., Ivarsson, B., Johnsson, B., Karlsson, R., Lundh, K., Lofas, S., Persson, B., Roos, H., Ronnberg, I., Sjolander, S., Stenberg, E., Stahlberg, R., Urbaniszky, C., Ostlin, H., and Malmqvist, M., 1991, Real-time biospecific interaction analysis using surfase plasmon resonance and a sensor chip technology, Bio Techniques 11: 620.Google Scholar
  15. Jung, C., Hui Bon Hoa, Schroeder, K.I., Simon, M., and Doucet, J.P., 1992, Substrate analogue induced changes of the CO-stretching mode in the cytochrome P450cam-carbon monooxide complex, Biochemistry 31: 1 2855.Google Scholar
  16. Kanaeva, I., Dedinskii, I., Skotselyas, E., Krainev, A., Guleva, I., Sevrukova, I., Koen, Y., Kuznetsova, G., Bachmanova, G., and Archakov, A.I., 1992, Comparative study of monomeric reconstituted and membrane microsomal monooxygenase systems of the rabbit liver. I. Properties of NADPH-cytochrome P450 reductase and cytochrome P450 LM2 (2B4) monomers, Arch. Biochem. Biophys. 298: 395.CrossRefGoogle Scholar
  17. Kanaeva, I.P., Nikitiyuk, O.V., Davydov, D.R., Dedinskii, I.R., Koen, Y.M., Kuznetsova, G.P., Skotselyas, E.D., Bachmanova, G.I.,and Archakov, A.I., 1992, Comparative study of monomeric reconstituted and membrane microsomal monooxygenase systems of the rabbit liver.II. Kinetic parameters of reductase and monooxygenase reactions, Arch. Biochem. Biophys. 298: 403.Google Scholar
  18. Karuzina, I I, Bachmanova, G.I., Mengazetdinov, D.R., Myasoedova, K.N., Zhikhareva, V.O., Kuznetsova, G.P., and Archakov, A.I., 1979, Isolation and characterization of cytochrome P450 from phenobarbital-induced rabbit liver microsomes, Biokhimia 44: 1049.Google Scholar
  19. Kanaeva, I.P., Skotselyas, E.D., Kuznetsova, G.P., Antonova, G.N., Bachmanova G.I., and Archakov, A.I., 1985, Reconstitution of liver monooxygenase cytochrome P-450 containing system by detergents in solution, Biokhimia 50: 1382.Google Scholar
  20. Lambeth, J.D., and Kriengsiri, S., 1985, Cytochrome P450scc - adrenodoxin interactions, J. Biol. Chem. 260: 8810.Google Scholar
  21. Lambeth, J.D., and Kamin, H., 1977, Steroidogenic electron transport by adrenodoxin reductase and adrenodoxin, J. Biol. Chem. 252: 2908.Google Scholar
  22. Lapko, A.G., Smettan, G., Ruckpaul, K., Usanov, S.A., 1991, Chemical modification of steroidhydroxylating monooxygenases with fluoresceinisothiocyanate, Bioorganicheskaya Khimiya 17: 921.Google Scholar
  23. Lepesheva, G.I., and Usanov, S.A., 1997, Dynamics and functional activity of cytochrome P450 selectively fluoresceinisothiocyanate-labeled, Biokhimia 62: 758.Google Scholar
  24. Lehnerer, M., Schulze, J., Petzold, A., Bernhardt, R., and Hlavica, P., 1995, Rabbit liver cytochrome P-450 2B5: high-level expression of the fuli-length protein in Escherichia co/i,purification and catalytic activity, Biochem. Biophys. Acta 1245: 107.CrossRefGoogle Scholar
  25. Nakamura, K., Horiuchi, T., Yasukochi, T., Sekimizu, K., Hara, T., and Sagara, Y., 1994, Significant contribution of arginine-112 and its positive charge of Pseudomonas putida cytochrome P-450cam in the electron transport from putidaredoxin, Biochem. Biophys. Acta 1207: 40.CrossRefGoogle Scholar
  26. Nishimoto, Y., and Otsuka-Murakami, H., 1988, Cytochrome b5, cytochrome c and cytochrome P450 interactions with NADPH-cytochrome P450 reductase in phospholipid vesicles, Biochemistry 27: 5869.CrossRefGoogle Scholar
  27. Omura, T., and Sato, R., 1964, The carbon monooxide binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. II. Solubilization, purification and properties, J. Biol. Chem. 239: 2370.Google Scholar
  28. Omura, T., and Takesue, S., 1970, A new method for simultaneous purification of cytochrome b5 and NADH-cytochrome b5 reductase from rat liver microsomes, J. Biochem. 67: 249.Google Scholar
  29. Ramsden, J.J., Bachmanova, G.I., and Archakov, A.I., 1994, Kinetic evidence for protein clustering at a surfase, Phys.Rev. 50: 5072.MathSciNetADSGoogle Scholar
  30. Ramsden, J.J., Bachmanova, G.I., and Archakov, A.I., 1996, Immobilisation of proteins to lipid bilayers, Biosensors and Bioelectronics 11: 523.CrossRefGoogle Scholar
  31. Roome, P.W., and Peterson, J.A., 1988, The oxidation of reduced putidaredoxin reductase by oxidized putidaredoxin, Arch. Biochem. Biophys. 266: 41.CrossRefGoogle Scholar
  32. Spatz, L., and Strittmatter, P., 1971, A form of cytochrome b5 that contain on additional hydrophobic sequence of 40 amino acid residiues, Proc. Natl. Acad. Sci. USA 68: 1042.ADSCrossRefGoogle Scholar
  33. Sevrukova, I.F., Kanaeva, I.P., Koen, Y.M., Samenkova, N.F., Bachmanova, G.I., and Archakov, A.I., 1994, Catalitic activity of cytochrome P4501 A2 in reconstituted system with emulgen 913, Arch. Biochem. Biophys. 310: 133.CrossRefGoogle Scholar
  34. Shymko, R.M., Gill, R., Wood, S., De Meyts, P., Ogawa Y., and Heding, A., 1994, Biosensor measurement of the kinetics of binding of IGF-I, IGF-Il,and IGF-I analogues to the IGF binding protein-3, in: Abstracts of 4-th European BlAsymposium on Biomolecular Interaction Analysis, Heidelberg, Germany 24.Google Scholar
  35. Tamburini, P.P., White, R.E., and Schenkman, J.B., 1985, Chemical characterization of protein-protein interactions between cytochrome P450 and cytochrome b5, J. Biol. Chem. 260: 4007.Google Scholar
  36. Voznesensky, A.I., and Shenkman, J.B., 1992, The cytochrome P4502B4-NADPH-cytochrome P450 reductase electron transfer complex is not formed by charge-pairing, J. Biol. Chem. 267: 14669.Google Scholar
  37. Wu, F.F., Vergeres, G., and Waskell, L., 1994, Kinetics of the reduction of cytochrome b5 with mutations in its membrane-binding domain, Arch. Biochem.Biophys. 308: 380.CrossRefGoogle Scholar
  38. Zhukov, A.,and Archakov, A., 1985, Stoichiometry of microsomal oxidation reactions. Distribution of reducing equivalents to monooxygenase and oxidase reactions catalyzed by cytochrome P-450, Biokhimia 50: 1939.Google Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Alexander I. Archakov
    • 1
  • Yuri D. Ivanov
    • 1
  1. 1.Institute of Biomedical ChemistryRAMSMoscowRussia

Personalised recommendations