Cytochrome P-450 spin state and leakiness of the monooxygenase pathway

References

• Archakov A. I., Zhukov A. A. Multiple activities of cytochrome P-450. Frontiers in Biotransformation, vol. 1: Basis and Mechanisms of Regulation of Cytochrome P-450, K. Ruckpaul, H. Rein. Akademie Verlag, Berlin 1989; 151–175
   Google Scholar
• Atkins W. M., Sugar S. G. The roles of active site hydrogen bonding in cytochrome P-450 CAM as revealed by site-directed mutagenesis. Journal of Biological Chemistry 1988; 263: 18844–18849
   Web of Science ®Google Scholar
• Atkins W. M., Sligar S. G. Molecular recognition in cytochrome P-450: alteration of regioselective alkane hydroxylation via protein engineering. Journal of the American Chemical Society 1989; 111: 2715–2717
   Web of Science ®Google Scholar
• Aust S. D., Roerig D. L., Pederson T. C. Evidence for superoxide generation by NADPH-cytochrome c reductase of rat liver microsomes. Biochemical and Biophysical Research Communications 1972; 47: 1133–1137
   PubMed Web of Science ®Google Scholar
• Beilsteins Handbuch der Organischen Chemie. Springer-Verlag, Berlin 1929/1973; Band 12, Hauptwerk, 1. 2. und 3. Ergänzungswerk
   Google Scholar
• Blanck J., Rein H., Sommer M., Ristau O., Smettan G., Ruckpaul K. Correlations between spin equilibrium shift, reduction rate, and N-demethylation activity in liver microsomal cytochrome P-450 and a series of benzphetamine analogues as substrates. Biochemical Pharmacology 1983; 32: 1683–1688
   PubMed Web of Science ®Google Scholar
• Bonfils C., Balny C., Maurel P. Direct evidence for electron transfer from ferrous cytochrome b5 to the oxyferrous intermediate of liver microsomal cytochrome P-450 LM2. Journal of Biological Chemistry 1981; 256: 9457–9465
   PubMed Web of Science ®Google Scholar
• Boveris A., Oshino N., Chance B. The cellular production of hydrogen peroxide. Biochemical Journal 1972; 128: 617–630
   PubMed Web of Science ®Google Scholar
• Debey P., Balny C. Production of superoxide ions in rat liver microsomes. Biochimie 1973; 55: 329–332
   PubMed Web of Science ®Google Scholar
• Ekström G., Ingelman-Sundberg M. Cytochrome P-450-dependent lipid peroxidation in reconstituted membrane vesicles. Biochemical Pharmacology 1984; 33: 2521–2523
   PubMed Web of Science ®Google Scholar
• Ekström G., Ingelman-Sundberg M. Mechanisms of lipid peroxidation dependent upon cytochrome P-450 LM2. European Journal of Biochemistry 1986; 158: 195–201
   PubMedGoogle Scholar
• Ekström G., Ingelman-Sundberg M. Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450 (P-450 IIE1). Biochemical Pharmacology 1989; 38: 1313–1319
   PubMed Web of Science ®Google Scholar
• Ekström G., Von Bahr C., Ingelman-Sundberg M. Human liver microsomal cytochrome P-450 IIE1. Immunological evaluation of its contribution to microsomal ethanol oxidation, carbon tetrachloride reduction and NADPH oxidase activity. Biochemical Pharmacology 1989; 38: 689–693
   PubMed Web of Science ®Google Scholar
• Estabrook R. W., Hildebrandt A. G., Baron J., Netter K. J., Leibman K. A new spectral intermediate associated with cytochrome P-450 function in liver microsomes. Biochemical and Biophysical Research Communications 1971; 42: 132–139
   PubMed Web of Science ®Google Scholar
• Estabrook R. W., Kawano S., Werringloer J., Kuthan H., Tsuji H., Graf H., Ullrich V. Oxycytochrome P-450: its breakdown to superoxide for the formation of hydrogen peroxide. Acta Biologica et Medica Germanica 1979; 38: 423–434
   PubMedGoogle Scholar
• Fridovich I., Handler P. Detection of free radicals generated during enzymic oxidations by the initiation of sulfite oxidation. Journal of Biological Chemistry 1961; 236: 1836–1840
   PubMed Web of Science ®Google Scholar
• Gillette J. R., Brodie B. B., LaDu B. N. The oxidation of drugs by liver microsomes: on the role of TPNH and oxygen. Journal of Pharmacology and Experimental Therapeutics 1957; 119: 532–540
   PubMed Web of Science ®Google Scholar
• Gorsky L. D., Coon M. J. Effects of conditions for reconstitution with cytochrome b5 on the formation of products in cytochrome P-450-catalyzed reactions. Drug Metabolism and Disposition 1986; 14: 89–96
   PubMed Web of Science ®Google Scholar
• Gorsky L. D., Koop D. R., Coon M. J. On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction. Journal of Biological Chemistry 1984; 259: 6812–6817
   PubMed Web of Science ®Google Scholar
• Guengerich F. P., Ballou D. P., Coon M. J. Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P-450. Biochemical and Biophysical Research Communications 1976; 70: 951–956
   PubMed Web of Science ®Google Scholar
• Guengerich F. P., Wang P., Davidson N. K. Estimation of isozymes of microsomal cytochrome P-450 in rats, rabbits, and humans using immunochemical staining coupled with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 1982; 21: 1698–1706
   PubMed Web of Science ®Google Scholar
• Gunsalus I. C., Meeks J. R., Lipscomb J. D., Debrunner P., Münck E. Bacterial monooxygenases-the P-450 cytochrome system. Molecular Mechanisms of Oxygen Activation, O. Hayaishi. Academic Press, New York 1974; 559–613
   Google Scholar
• Hildebrandt A. G., Roots I. Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Archives of Biochemistry and Biophysics 1975; 180: 343–347
   Google Scholar
• Hildebrandt A. G., Speck M., Roots I. Possible control of hydrogen peroxide production and degradation in microsomes during mixed function oxidation reaction. Biochemical and Biophysical Research Communications 1973; 54: 968–975
   PubMed Web of Science ®Google Scholar
• Hildebrandt A. G., Heinemeyer G., Roots I. Stoichiometric cooperation of NADPH and hexobarbital in hepatic microsomes during the catalysis of hydrogen peroxide formation. Archives of Biochemistry and Biophysics 1982; 216: 455–465
   PubMed Web of Science ®Google Scholar
• Van Der Hoeven T. A., Coon M. J. Preparation and properties of partially purified cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase from rabbit liver microsomes. Journal of Biological Chemistry 1974; 249: 6302–6310
   PubMed Web of Science ®Google Scholar
• Imai Y. The roles of cytochrome b5 in reconstituted monoxygenase systems containing various forms of hepatic microsomal cytochrome P-450. Journal of Biochemistry 1981; 89: 351–362
   PubMed Web of Science ®Google Scholar
• Imai Y., Sato R. The role of cytochrome b5 in a reconstituted N-demethylase system containing cytochrome P-450. Biochemical and Biophysical Research Communications 1977; 75: 420–426
   PubMed Web of Science ®Google Scholar
• Imai M., Shimada H., Watanabe Y., Matsushima-Hibiya Y., Makino R., Koga H., Horiuchi T., Ishimura Y. Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: a possible role of the hydroxy amino acid in oxygen activation. Proceedings of the National Academy of Sciences, USA 1989; 86: 7823–7827
   PubMed Web of Science ®Google Scholar
• Ingelman-Sundberg M., Johansson I. Cytochrome b5 as electron donor to rabbit liver cytochrome P-450 LM2 in reconstituted phospholipid vesicles. Biochemical and Biophysical Research Communications 1980; 97: 582–589
   PubMed Web of Science ®Google Scholar
• Ingelman-Sundberg M., Johansson I. Mechanisms of hydroxyl radical formation and ethanol oxidation by ethanol-inducible and other forms of rabbit liver microsomal cytochromes P-450. Journal of Biological Chemistry 1984; 259: 6447–6458
   PubMed Web of Science ®Google Scholar
• Iyanagi T., Suzaki T., Kobayashi S. Oxidation-reduction states of pyridine nucleotide and cytochrome P-450 during mixed-function oxidation in perfused rat liver. Journal of Biological Chemistry 1981; 256: 12933–12939
   PubMed Web of Science ®Google Scholar
• Jansson I., Schenkman J. B. Influence of cytochrome b5 on the stoichiometry of the different oxidative reactions catalyzed by liver microsomal cytochrome P-450. Drug Metabolism and Disposition 1987; 15: 344–348
   PubMed Web of Science ®Google Scholar
• Kuthan H., Ullrich V. Oxidase and oxygenase function of the microsomal cytochrome P-450 monooxygenase system. European Journal of Biochemistry 1982; 126: 583–588
   PubMedGoogle Scholar
• Kuthan H., Tsuji H., Graf H., Ullrich V. Generation of superoxide anion as a source of hydrogen peroxide in a reconstituted monooxygenase system. FEBS Letters 1978; 91: 343–345
   PubMed Web of Science ®Google Scholar
• Nash T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochemical Journal 1953; 55: 416–421
   PubMed Web of Science ®Google Scholar
• Nordblom G. D., Coon M. J. H2O2 formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450. Archives of Biochemistry and Biophysics 1977; 180: 343–347
   PubMed Web of Science ®Google Scholar
• Oprian D. D., Gorsky L. D., Coon M. J. Properties of the oxygenated form of liver microsomal cytochrome P-450. Journal of Biological Chemistry 1983; 258: 8684–8691
   PubMed Web of Science ®Google Scholar
• Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. Journal of Biological Chemistry 1964; 239: 2370–2378
   PubMed Web of Science ®Google Scholar
• Peterson J. A. Camphor binding by pseudomonas putida cytochrome P-450. Archives of Biochemistry and Biophysics 1971; 144: 678–693
   Web of Science ®Google Scholar
• Petzold D. R., Rein H., Schwarz D., Sommer M., Ruckpaul K. Relation between the structure of benzphetamine analogues and their binding properties to cytochrome P-450 LM2. Biochimica et Biophysica Acta 1985; 829: 253–261
   PubMed Web of Science ®Google Scholar
• Ristau O. Ein Computerprogramm zur implizierten Regression der Hillgleichung. Acta Biologica et Medica Germanica 1975; 34: 313–318
   PubMedGoogle Scholar
• Ruckpaul K., Rein H., Blanck J. Regulation mechanisms of the activity of the hepatic endoplasmic cytochrome P-450. Frontiers in Biotransformation, vol. 1: Basis and Mechanisms of Regulation of Cytochrome P-450, K. Ruckpaul, H. Rein. Akademie Verlag, Berlin 1989; 1–65
   Google Scholar
• Schwarze W., Blanck J., Ristau O., Jänig G.-R., Pommerening K., Rein H., Ruckpaul K. Spin state control of cytochrome P-450 reduction and catalytic activity in a reconstituted P-450 LM2 system as induced by a series of benzphetamine analogues. Chemico-Biological Interactions 1985; 54: 127–141
   PubMed Web of Science ®Google Scholar
• Soodaeva S. K., Skotzelyas E. D., Zhukov A. A., Archakov A. I. Comparative studies of superoxide radical generation in microsomes and reconstituted monooxygenase systems. Cytochrome P-450, Biochemistry, Biophysics, and Environmental Implications, E. Hietanen, M. Laitinen, O. Hänninen. Elsevier, Amsterdam 1982; 615–618
   Google Scholar
• Staudt H., Lichtenberger F., Ullrich V. The role of NADH in uncoupled microsomal monooxygenations. European Journal of Biochemistry 1974; 46: 99–106
   PubMedGoogle Scholar
• Takemori S., Wada K., Ando K., Hosokawa H. Studies on cytochrome a. VIII. Reaction of cytochrome a with chemically modified cytochrome c and basic proteins. Journal of Biochemistry (Tokyo) 1962; 52: 28–37
   PubMed Web of Science ®Google Scholar
• Tamburini P. P., Gibson G. G. Thermodynamic studies of the protein-protein interactions between cytochrome P-450 and cytochrome b5. Evidence for a control role of the cytochrome P-450 spin state in the coupling of substrate and cytochrome b5-binding to the terminal hemoprotein. Journal of Biological Chemistry 1983; 258: 13444–13452
   PubMed Web of Science ®Google Scholar
• Terelius Y., Ingelman-Sundberg M. Cytochrome P-450-dependent oxidase activity and hydroxyl radical production in micellar and membraneous types of reconstituted systems. Biochemical Pharmacology 1988; 37: 1383–1389
   PubMed Web of Science ®Google Scholar
• Thurman R. G., Ley H. G., Scholz R. Hepatic microsomal ethanol oxidation. Hydrogen peroxide formation and the role of catalase. European Journal of Biochemistry 1972; 25: 420–430
   PubMedGoogle Scholar
• Tindberg N., Ingelman-Sundberg M. Cytochrome P-450 and oxygen toxicity. Oxygen-dependent induction of ethanol-inducible cytochrome P-450 (IIE1) in rat liver and lung. Biochemistry 1989; 28: 4499–4504
   PubMed Web of Science ®Google Scholar
• Tuckey R. C., Kamin H. Theoxyferro complex of adrenal cytochrome P-450 SCC. Effect of cholesterol and intermediates on its stability and optical characteristics. Journal of Biological Chemistry 1982; 257: 9309–9314
   PubMed Web of Science ®Google Scholar
• Werringloer J., Kawano S. The control of the cyclic function of liver microsomal cytochrome P-450: -Counterpoise’-regulation of the electron transfer reactions required for the activation of molecular oxygen. Biochemistry, Biophysics and Regulation of Cytochrome P-450, J. A. Gustafsson, J. Carlstedt-Duke, A. Mode, J. Rafter. Elsevier/North-Holland, Amsterdam 1980; 359–362
   Google Scholar
• Werringloer J., Kawano S., Estabrook R. W. Spin state transitions of liver microsomal cytochrome P-450. Acta Biologica et Medica Germanica 1979; 38: 163–175
   PubMedGoogle Scholar
• Zhukov A. A., Archakov A. I. Complete stoichiometry of free NADPH oxidation in liver microsomes. Biochemical and Biophysical Research Communications 1982; 109: 813–818
   PubMed Web of Science ®Google Scholar
• Zhukov A. A., Archakov A. I. Stoichiometry of the reactions of microsomal oxidation. Distribution of redox equivalents between monooxygenase and oxidase reactions catalyzed by cytochrome P-450. Biochemistry (USSR) 1985; 50: 1659–1672
   Web of Science ®Google Scholar