Abstract
The main concern of these lectures is: Do liver microsomal cytochromes P-450 have an oligomeric structure and is cooperativity involved in their function? Elements of topology of membrane proteins and the spectroscopic techniques used to investigate this toplogy are described. Oligomeric structure is an important element of membrane topology and information on it can be obtained from measurements of rotational diffusion of the proteins. Emphasis is therefore laid on photoselection techniques (time-dependent polarized delayed fluorescence and phosphorescence and time-dependent absorption dichroism).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
M.L. Jennings, Topography of membrane proteins, Annu. Rev. Biochem. 58: 999 (1989).
K.U. Linderstrøm-Lang and J.A. Schellrnan, Protein structure and enzyme activity, in “The Enzymes”, P.D. Boyer, H. Lardy, and K. Myrbäck, eds., Academic Press, New York (1959).
A. Stier and S.A.E. Finch, Rotational diffusion of homo-and heterooligomers of cytochrome P-450: the functional significance of cooperativity and the membrane structure, in: “Frontiers in Biotransformation”, Vol. 1, K. Ruckpaul and H. Rein, eds., Taylor & Francis, London, submitted.
J.R. Abney and J.C. Owicki, Theories of protein-lipid and protein-protein interactions in membranes, in: “Progress in Protein-Lipid Interactions”, Vol. 1, A. Watts and J.J.H.H.M. De Pont, eds., Elsevier Science Publishers, Amsterdam (1985).
I. Klotz, D.W. Darnall, and N.R. Langerman, Quaternary structure of proteins, in: “The Proteins”, Vol. 1, H. Neurath and R.L. Hill, eds, Academic Press, New York (1975).
D.E. Koshland Jr., G. Nemethy, and D. Filmer, Comparison of experimental binding data and theoretical models in proteins containing subunits, Biochemistry 5: 365 (1966).
D. Marsh, Molecular mobility in membranes, in: “Physical Properties of Biological Membranes and Their Functional Implications”, C. Hidalgo, ed., Plenum Publishing Company, New York (1988).
H. Sandermann Jr., Cooperativity of lipid-protein interactions, in: “Progress in Protein-Lipid Interactions” Vol. 2, A. Watts and J.J.H.H.M. De Pont, eds., Elsevier Science Publishers, Amsterdam (1986).
H. Frauenfelder, F. Parak, and R.D. Young, Conformational substates in proteins, Annu. Rev. Biophys. Biophys. Chem. 17: 451 (1988).
C. Jung, F. Marlow, O. Ristau, S. Falsett. I.C. Gunsalus, and H. Frauenfelder, Accessibility and dynamics of the active site in bacterial cytochrome P-450, in: “Cytochrome P-450: Biochemistry and Biophysics”, I. Schuster, ed. Taylor & Francis, London (1989).
J. Monod, J. Wyman, and J.-P. Changeaux, On the nature of allosteric transitions: A plausible model, J. Mol. Biol. 12: 88 (1965).
G.R. Welch (ed.) “Organized Multienzyme Systems: Catalytic Properties”, Academic Press Inc., Orlando (1985).
E. Sackmann and H. Träuble, Studies of the crystalline-liquid crystalline phase transition of lipid model membranes. II. Analysis of the electron spin resonance spectra of steroid labels incorporated into lipid membranes, J. Am. Chem. Soc. 94: 4491 (1972).
H. Träuble and E. Sackmann, Studies of the crystalline-liquid crystalline phase transition of lipid model membranes. III. Structure of a steroid-lecithin system below and above the lipid phase transition, J. Am. Chem. Soc. 94: 4499 (1972).
C.J. Scandella, P. Devaux, and H.M. McConnell, Rapid lateral diffusion of phospholipids in rabbit sarcoplasmic reticulum. Proc. Natl. Acad. Sci USA 69: 2056 (1972).
M. Edidin, Rotational and translational diffusion in membranes, Annu. Rev. Biophys. Bioeng. 3: 179 (1974).
M.D. Hollenberg, Examples of homospecific and heterospecific receptor regulation, Trends Pharmacol. Sci. 6: 242 (1985).
J. Schlessinger, Signal transduction by allosteric receptor oligomerization, Trends Biochem. Sci. 13: 443 (1988).
J.-P. Changeux, A. Devillers-Thiery, and P. Chemouilli, Acetylcholine receptor: An allosteric protein, Science 225: 1355 (1984).
C.R. Hackenbrock, B. Chazotte, and S.S. Gupte, The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport, J. Bioenerg. Biomembr. 18: 331 (1986).
J.W. DePierre and L. Ernster, Enzyme topology of intracellular membranes, Ann. Rev. Biochem. 46: 201 (1977).
M. Ingelman-Sundberg, Cytochrome P-450 organization and membrane interaction,, in: “Cytochrome P-450”, P.R. Ortiz de Montellano, ed., Plenum Press, New York (1986).
E. Schulz, A critical evaluation of methods for prediction of protein secondary structures, Annu. Rev. Biophvs. Biophvs. Chem. 17: 1 (1988).
B.A. Wallace, M. Cascio, and D.L. Mielke, Evaluation of methods for the prediction of membrane protein secondary structures, Proc. Natl. Acad. Sci. USA 83: 9423 (1986).
G.E. Tarr, S.D. Black, V.S. Fujita, and M.J. Coon, Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes, Proc. Natl. Acad. Sci. USA 80: 6552 (1983).
A. M. Lesk and C. Chothia, How different amino acid sequences determine similar protein structure: the structure and evolutionary dynamics of the globins, J. Mol. Biol. 136: 225 (1980).
C. Chothia and A.M. Lesk, Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family, J. Mol. Biol. 182: 151 (1985).
C. De Lemos-Chiarandini, A.B. Frey, D.D. Sabatini and G. Kreibich, Determination of the membrane topology of the phenobarbital-inducible rat liver cytochrome P-450 isoenzyme PB-4 using site-specific antibodies, J. Cell Biol. 104: 209 (1987).
R. Müller, W.E. Schmidt, and A. Stier, The site of cyclic AMP-dependent protein kinase catalyzed phosphorylation of cytochrome P-450 LM2. FEBS Lett. 187: 21 (1985).
H. Furuya, T. Shimizu, K. Hirano, M. Hatano, Y. Fujii-Kuriyama, R. Raag, and T.L. Poulos, Site-directed mutageneses of rat liver cytochrome P-450d: catalytic activities toward benzphetamine and 7-ethoxycoumarin, Biochemistry: 28: 6848 (1989).
J. Murakami, Y. Yabusaki, T. Sakaki, M. Shibata, and H. Ohkawa, A genetically engineered P-450 monooxygenase: Construction of the functional fused enzyme between rat cytochrome P-450c and NADPH-cytochrome P-450 reductase, DNA 6: 189 (1987).
E.S. Kempner and W. Schlegel, Size determination of enzymes by radiation inactivation, Analvt. Biochem. 92: 2 (1979).
E.S. Kempner and J.H. Miller, Radiation inactivation of glutamate dehydrogenase hexamer: lack of energy transfer between subunits, Science 222: 586 (1983).
F.P. Guengerich, P.F. Churchill, C.Y. Jung and S. Fleischer, Target inactivation analysis applied to determination of rat liver proteins in the purified state and in microsomal membranes, Biochim. Biophvs. Acta 915: 246 (1987).
J. Deisenhofer, O. Epp, K. Miki, R. Huber, and H. Michel, structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 A resoluton, Nature 318: 618 (1985).
K. Moffat, Time-resolved macromolecular crystallography, Annu. Rev. Biophys. Biophys. Chem. 18: 309 (1989).
P. Fajer and D. Marsh, Sensitivity of saturation transfer ESR spectra to anisotropic rotation. Application to membrane systems, J. Magn. Reson. 51: 446 (1983).
D.D. Thomas, T.M. Eads, V.A. Barnett, K.M. Lindahl, D.A. Momont, and T.C. Squier, Saturation transfer EPR and triplet anisotropy: Complementary techniques for the study of microsecond rotational dynamics, in: “Spectroscopy and the Dynamics of Molecular Biological Systems”, P.M. Bayley, R.E. Dale, eds., Academic Press, London, (1985).
D. Schwarz, J. Pirrwitz, and K. Ruckpaul, Rotational diffusion of cytochrome P-450 in the microsomal membrane — evidence for a clusterlike organization from saturation transfer electron paramagnetic resonance spectroscopy, Archives Biochem. Biophys. 216: 322 (1982).
R.M. Cooke and I.D. Campbell, Protein structure determination by nuclear magnetic resonance, Bio Essays 8: 52 (1988)
A. Bax, Two-dimensional NMR and protein structure, Annu. Rev. Biochem. 58: 223 (1989).
K. Wüthrich, “NMR of proteins and nucleic acids”, Wiley, New York (1986).
S.O. Smith and R.G. Griffin, High-resolution solid-state NMR of proteins, Annu Rev. Phys. Chem. 39: 511 (1988).
R. Smith, D.E. Thomas, F. Separovic, A.R. Atkins, and B.A. Cornell, Determination of the structure of a membraneincorporated ion channel, Biophys. J. 56: 307 (1989).
T.M. Jovin and W.L.C. Vaz, Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods, Methods. Enzymol. 172: 471 (1989).
R. Greinert, H. Staerk, A. Stier, and A. Weiler, E-type delayed fluorescence depolarization, a technique to probe rotational motion in the microsecond range. J. Biochem. Biophvs. Methods. 1: 77 (1979).
R. Greinert and A. Stier, Rotational diffusion of cytochrome P-450 in a reconstituted system measured by depolarization of delayed fluorescence, in: “Biochemistry, Biophysics and Regulation of Cytochrome P-450”, J.Å. Gustafsson, J. Carlstedt Duke, A. Mode, and J. Rafter, eds., Biomedical Press, Elsevier/North-Holland (1980).
R. Greinert, S.A.E. Finch, and A. Stier, Cytochrome P-450 rotamers control mixed-function oxygenation in reconstituted membranes. Rotational diffusion studied by delayed fluorescence depolarization. Xenobiotica 12: 717 (1982a).
R. Greinert, S.A.E. Finch, and A. Stier, Conformation and rotational diffusion of cytochrome P-450 changed by substrate binding. Biosci. Rep. 2: 991 (1982b).
R.J. Cherry, Transient dichroism of bacteriorhodopsin, Methods Enzymol. 88: 248 (1982).
W.L.C. Vaz, R.H. Austi, and H. Vogel, The rotational diffusion of cytochrome b5 in lipid bilayer membranes, Biophvs.J. 26:415 (1979)
P. Roesen and A. Stier, Kinetics of CO and 02 complexes of rabbit liver microsomal cytochrome P450, Biochem. Biophys. Res. Commun. 51: 603 (1973).
F. Mitani, T. Iizuka, H. Shimada, R. Ueno, and Y. Ishimura, Flash photolysis studies on the CO complexes of ferrous cytochrome P-450scc and cytochrome P-45011β, J. Biol. Chem. 260: 12042 (1985).
C. Richter, K.H. Winterhalter, and R.J. Cherry, Rotational diffusion of cytochrome P-450 in rat liver microsomes, FEBS Lett. 102: 151 (1979).
S. Kawato, J. Gut, R.J. Cherry, K.H. Winterhalter, and C. Richter, Rotation of cytochrome P-450. I. Invetigation of protein-protein interaction of cytochrome P-450 in phospholipid vesicles and liver microsomes, J, Biol. Chem. 257: 7023 (1982).
J. Gut, C. Richter, R.J. Cherry, K.H. Winterhalter, and S. Kawato, Rotation of cytochrome P-450. II. Specific interactions of cytochrome P-450 with NADPH-cytochrome P-450 reductase in phospholipid vesicles, J. Biol. Chem. 257: 7030 (1982).
C.A. Parker, “Photoluminescence of Solutions”, Elsevier, Amsterdam (1968).
S. Kawato and K. Kinosita, Time-dependent absorption anisotropy and rotational diffusion of proteins in membranes, Biophvs.J. 36: 277 (1981).
K. Kinosita Jr., A. Ikegami, and S. Kawato, On the wobbling-in-cone analysis of fluorescence anisotropy decay. Biophys. J. 37: 461 (1982).
B.D. Hughes, B.A. Pailthorpe, L.T. White, and W.H. Sawyer, Extraction of membrane microvisosity from translational and rotational diffusion coefficients, Biophys. J. 37: 673 (1982).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Plenum Press, New York
About this chapter
Cite this chapter
Stier, A., Krüger, V., Eisbein, T., Finch, S.A.E. (1991). Membrane Topology of Cytochromes P-450: Elements and Measurement by Spectroscopic Techniques. In: Arinç, E., Schenkman, J.B., Hodgson, E. (eds) Molecular Aspects of Monooxygenases and Bioactivation of Toxic Compounds. NATO ASI Series Advanced Science Institutes Series, vol 202. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7284-4_6
Download citation
DOI: https://doi.org/10.1007/978-1-4684-7284-4_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-7286-8
Online ISBN: 978-1-4684-7284-4
eBook Packages: Springer Book Archive