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Research Article

The Mechanism of Hydrocarbon Oxidation by a Corynebacterium Species

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Pages 239-289 | Published online: 25 Sep 2008

References

  • ZoBell C. E. Action of microorganisms on hydrocarbons. Bact. Rev. 1946; 10: 1
  • ZoBell C. E. Assimilation of hydrocarbons by microorganisms. Advances Enzym. 1950; 10: 433
  • Beerstecher E., Jr. Petroleum Microbiology. Elsevier Press, Houston 1954
  • Fúhs G. W. Der mickrobielle Abbau von Kohlenwasserstoffen. Arch. Mikrobiol. 1961; 39: 374
  • Davis J. B., Updegraff D. M. Microbiology in the petroleum industry. Bact. Rev. 1954; 18: 215
  • Davis J. B. Petroleum Microbiology. Elsevier Publishing Co., Amsterdam 1967
  • Foster J. W. Bacterial oxidation of hydrocarbons. Oxygenases, O. Hayaishi. Academic Press, New York 1962
  • Foster J. W. Hydrocarbons as substrates for microorganisms. Antonie Leeuwenhoek 1962; 28: 241
  • Van der Linden A. C., Thijsse G. J. E. The mechanism of microbial oxidations of petroleum hydrocarbons. Advances Enzym. 1965; 27: 469
  • McKenna E. J., Kallio R. E. The biology of hydrocarbons. Ann. Rev. Microbiol. 1965; 19: 183
  • Dagley S., Evans W. C., Ribbons D. W. New pathways in the oxidative metabolism of aromatic compounds by microorganisms. Nature 1960; 188: 560
  • Ragoff M. H. Oxidation of aromatic compounds by bacteria. Advances Appl. Microbiol. 1961; 3: 193
  • Evans W. C. The microbiological degradation of aromatic compounds. J. Gen. Microbiol. 1963; 32: 177
  • Treccani V. Microbial degradation of hydrocarbons. Progr. Industr. Microbiol. 1964; 4: 3
  • Hayaishi O. Oxygenases. Proceedings 6th Intern. Cong. Biochem. New York 1964; 31, Plenary Session, 33
  • Hayaishi O. Crystalline oxygenases of pseudomonads. Bacter. Rev. 1966; 30: 720
  • Gibson D. T. Microbial, degradation of aromatic compounds. Science 1968; 161: 1093
  • Lebeault J. M., Lode E. T., Coon M. J. Fatty acid and hydrocarbon hydroxylation in yeasts: Role of cytochrome P-450 in Candida tropicalis. Biochem. Biophys. Res. Commun. 1971; 42: 413
  • Kester A. S. Studies on the oxidation of hydrocarbons by microorganisms. Ph.D. Dissertation, University of Texas, Austin, Texas 1961
  • Leadbetter E. R., Foster J. W. Studies on some methane-utilizing bacteria. Arch. Mikrobiol. 1958; 30: 91
  • Kester A. S., Foster J. W. Ditérminal oxidation of long chain alkanes by bacteria. J. Bact. 1963; 85: 859
  • Gordon R. E. Some strains in search of a genus-Corynebacterium, Mycobacterium, Nocardia or what?. J. Gen. Microbiol. 1966; 43: 329
  • Veldkamp H. Saprophytic coryneform bacteria. Ann. Rev. Microbiol. 1970; 24: 209
  • Harrington B. J. A numerical taxonomical study of some Cornyebacteria and related organisms. J. Gen. Microbiol. 1966; 45: 31
  • Jensen H. L. Studies on saprophytic Mycobacteria and Corynebacteria. Proc. Linnean Soc. London, N.S.W. 1934; LIX: 19
  • Mandel M. 1968, Personal communication
  • Lukins H. B., Foster J. W. Utilization of hydrocarbons and hydrogen by mycobacteria. Z. Allg. Mikrobiol. 1963; 3: 251
  • Söhngen N. L. Benzin, petroleum, paraffinöl und paraffin als kohlen stoff-und energiequelle für microben. Zentr. Bakteriol. Parasitenk. 1913; 37: 595, Abt. II
  • Büttner H. Zur kenntnis der Mykobacterien, insbesondere ihres quantitativen stoffwechsel auf paraffin-nahnboden. Arch. Hyg. Bacteriol. 1926; 97: 12
  • Haag F. E. Die saprophytischen Mykobacterien. Zentrabl. Bakteriol. Parasitenk. 1927; 71: 1, Abt. II
  • Gordon R. E., Hagan W. A. The isolation of acid-fast bacteria from soil. Amer. Rev. Tuberc. 1937; 36: 549
  • Buswell J. A., Jurtshuk P. Microbial oxidation of hydrocarbons measured by oxygraphy. Arch. Mikrobiol. 1969; 64: 215
  • Lowery C. E., Jr., Foster J. W., Jurtshuk P. The growth of various filamentous fungi and yeasts on n-alkanes and ketones. 1. Studies on substrate specificity. Arch. Mikrobiol. 1968; 60: 246
  • Kahn M. Y. A., Hall A. N., Robinson D. S. Microbial transformation of n-octane into dicarboxylic acids. Nature 1963; 198: 289
  • Kusunose M., Kusunose E., Coon M. J. Enzymatic ω-oxidation of fatty acids. I. Products of octanoate, decanoate and Iaurate oxidation. J. Biol. Chem. 1964; 239: 1374
  • Kusunose Kusunose M. E., Coon M. J. Enzymatic ω-oxidation of fatty acids. II. Substrate specificity and other properties of the enzyme system. J. Biol. Chem. 1964; 239: 2135
  • Robbins K. C. In vitro enzymic omega oxidation of medium chain fatty acids in mammalian tissue. Arch. Biochem. 1968; 123: 531
  • Verkade P. E., Van der Lee J. Researches on fat metabolism. II. Biochem. J. 1934; 28: 31
  • Lu A. Y. H., Junk K. W., Coon M. J. Resolution of the cytochrome P-450 containing ω-hydroxylarion system of liver microsomes into three components. J. Biol. Chem. 1969; 244: 3714
  • Cardini G., Jurtshuk P. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J. Biol. Chem. 1970; 245: 2789
  • Friedel R. A., Shultz J. L., Sharkey A. G. Mass spectra of alcohols. Anal. Chem. 1956; 28: 926
  • Cardini G., Jurtshuk P. Cytochrome P-450 involvement in the oxidation of n-octane by cell-free extracts of Corynebacterium sp. strain 7E1C. J. Biol. Chem. 1968; 243: 6071
  • Gornall A. G., Bardawill C. J., David M. M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 1949; 177: 751
  • Stewart J. E., Kallio R. E., Stevenson D. P., Jones A. G., Schissler D. O. Bacterial hydrocarbon oxidation. 1. Oxidation of n-hexadecane by a gram-negative coccus. J. Bact. 1959; 78: 441
  • Leadbetter E. R., Foster J. W. Incorporation of molecular oxygen in bacterial cells utilizing hydrocarbons for growth. Nature 1959; 184: 1428
  • Lukins H. B., Foster J. W. Methyl ketone metabolism in hydrocarbon utilizing mycobacteria. J. Bact. 1963; 85: 1074
  • Cohn M., Urey H. C. Oxygen exchange reactions of organic compounds and water. J. Amer. Chem. Soc. 1938; 60: 679
  • Baptist J. N., Gholson R. K., Coon M. J. Hydrocarbon bacterial enzyme system. I. Products of octane oxidation. Biocheim. Biophys. Acta 1963; 69: 40
  • Gholson R. K., Baptist J. N., Coon M. J. Hydrocarbon oxidation by a bacterial enzyme system. II. Cofactor requirements for octanol formation from octane. Biochemistry 1963; 2: 1155
  • Leadbetter E. R., Foster J. W. Bacterial oxidation of gaseous alkanes. Arch. Mikrobiol. 1960; 35: 92
  • Tanabe M., Dehn R. L., Kuo M. H. Microbial oxidation of p-diefhylbenzene. Biochemistry 1971; 10: 1087
  • Sladek N. E., Mannering G. J. Evidence for a new P-450 hemoprotein in hepatic microsomes from methylcholanthrene treated rats. Biochem. Biophys. Res. Commun. 1966; 24: 668
  • Kupfer D. Enzyme induction by drugs. Bioscience 1970; 20: 705
  • Azoulay E., Senez J. C. Deshydrogenation d'hydrocarbures paraffiniques, en presence de pyocyanine, par des extraits de Pseudomonas aeruginosa. Compt. Rend. 1958; 247: 1251
  • Senez J. C., Azoulay E. Deshydrogenation d'hydrocarbures paraffiniques par les suspensions non-proliferantes et les extraits de Pseudomonas aeruginosa. Biochim. Biophys. Acta 1961; 47: 307
  • Chouteau J., Azoulay E., Senez J. C. Anaerobic formation of n-hept-1-ene from n-heptane by resting cells of Pseudomonas aeruginosa. Nature 1962; 194: 577
  • Azoulay E., Chouteau J., Davidovics G. Isolement et caracterisation des enzymes responsibles de l'oxydation deshydrocarbures. Biochim. Biophys. Acta 1963; 77: 554
  • Cardini G. The hydroxylation of n-octane by a cell-free extract of Corynebacterium 7E1C. Ph.D. dissertation, University of Texas, Austin 1969
  • Cardini G., Jurtshuk P., Unpublished data
  • Jorgensen J. A., Kester A. S. 1971, Personal communication
  • Ciegler A. Microbial carotenogenesis. Advances Appl. Microbiol. 1965; 7: 1
  • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 1964; 239: 2370
  • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification and properties. J. Biol. Chem. 1964; 239: 2379
  • Estabrook R. W., Schenkman J. B., Cammer W., Remmer H., Cooper D. Y., Narasimhulu S., Rosenthal O. Cytochrome P-450 and mixed function oxidations. Biological and Chemical Aspects of Oxygenases, K. Bloch, O. Hayashi. Maruzen Co., Ltd., Tokyo 1966
  • Omura T., Sato R. Isolation of cytochromes P-450 and P-420. Methods in Enzymology, R. E. Estabrook, M. E. Pullman. Academic Press, New York 1967; Vol. X
  • Miyake Y., Gaylor J. H., Mason H. S. Properties of a submicrosomal particle containing P-450 and a flavoprotein. J. Biol. Chem. 1968; 243: 5788
  • Lu Y. H., Coon M. J. Role of hemoprotein P-450 in fatty acid ω-hydroxylation in a soluble enzyme system from liver microsomes. J. Biol. Chem. 1968; 243: 1331
  • Strobel H. W., Lu A. Y. H., Heideman J., Coon M. J. Phosphatidylcholine requirement in the enzymatic reduction of hemoprotein P-450 in fatty acid, hydrocarbon and drug hydroxylation. J. Biol. Chem. 1970; 245: 4851
  • Margoliash E. Use of ion exchanges in the preparation and purification of cytochrome c. Biochem. J. 1954; 56: 529
  • Ziegler D. M., Doeg K. A. Studies on the electron transport system. XLIII. The isolation of a succinic-coenzyme Q reductase from beef heart mitochondria. Arch. Biochem. 1962; 97: 41
  • Horecker B. L., Kornberg A. The extinction coefficients of the reduced band of pyridine nucleotides. J. Biol. Chem. 1948; 175: 385
  • Hatefi Y., Haavik A. G., Griffiths D. E. Reconstitution of the electron transport system. I. Preparation and properties of the interacting enzyme complexes. Biochem. Biophys. Res. Commun. 1961; 4: 441
  • Sato R., Omura T., Nishibayashi H. Carbon monoxide-binding NADH-specific flavoprotein in liver microsomes and their roles in microsomal electron transfer. Oxidases and Related Redox Systems, T. E. King, H. S. Mason, M. Morrison. John Wiley and Sons, New York 1965; VoL II
  • Mason H. S., North J. C., Vanneste M. Microsomal mixed-function oxidations: The metabolism of xenobiotics. Fed. Proc. 1965; 24: 1172
  • Cooper D. Y., Narasimhulu S., Rosenthal O., Estabrook R. W. Spectral and kinetic studies of microsomal pigments. Oxidases and Related Redox Systems, T. E. King, H. S. Mason, M. Morrison. John Wiley and Sons, New York 1965; Vol. II
  • Mason H. S., Yamano T., North J. C., Hashimoto Y., Sakagishi P. The structure and oxidase function of liver microsomes. Oxidases and Related Redox Systems, T. E. King, H. S. Mason, M. Morrison. John Wiley and Sons, New York 1965; Vol. II
  • Ernster L., Orrenius S. Substrate-induced synthesis of the hydroxylating enzyme system of liver microsomes. Fed. Proc. 1965; 24: 1190
  • Orrenius S., Ericsson J. L. E., Ernster L. Phenobarbital induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic membranes. J. Cell Biol. 1967; 25: 627
  • Brown R. R., Miller J. A., Miller E. C. The metabolism of methylated aminoazo dyes. IV. Dietary factors enhancing demethylation in vitro. J. Biol. Chem. 1954; 228: 211
  • Conney A. H., Miller E. C., Miller J. A. Substrate-induced synthesis and other properties of benzpyrene hydroxylase in rat liver. J. Biol. Chem. 1957; 228: 753
  • Conney A. H., Gilman A. G. Puromycin inhibition of enzyme by 3-methylcholanthrene and phenobarbital. J. Biol. Chem. 1963; 238: 3682
  • Remmer H., Merker H. J. Drug-induced changes in the liver endoplasmic reticulum: Association with drug metabolizing enzymes. Science 1963; 142: 1657
  • Symposium on Electron Transport Systems in Microsomes. 49th Ann. Meeting Fed. of American Soc. Exper. Biol., Atlantic City, New Jersey, Fed. Proc., 24, 1153, 1965
  • Oxidases and Related Redox Systems, T. E. King, H. S. Mason, M. Morrison. John Wiley and Sons, New York 1965; Vols. I and II
  • Biological and Chemical Aspects of Oxygenases, K. Block, O. Hayaishi. Maruzen Co., Tokyo 1966
  • Microsomes and Drug Oxidations, J. R. Gillette, A. H. Conney, G. J. Cosmides, J. R. Estabrook, G. J. Mannering. Academic Press, New York 1969
  • Drug Metabolism in Man. Ann. N. Y. Acad. Sci. 1971; 179, Vesell E. S., Eds.
  • Mason H. S. Mechanisms of oxygen metabolism. Advances Enzym. 1957; 19: 79
  • Mason H. S. Oxidases. Ann. Rev. Biochem. 1965; 34: 595
  • Hayaishi O. History and scope. Oxygenases, O. Hayaishi. Academic Press, New York 1962
  • Mason H. S., Fowlks W. L., Peterson E. Oxygen transfer and electron transport by the phenolase complex. J. Am. Chem. Soc. 1955; 77: 2914
  • Hayaishi O., Katagiri M., Rothberg S. Mechanism of the pyrocatechase reaction. J. Am. Chem. Soc. 1955; 77: 5450
  • Peterson J. A., Basu D., Coon M. J. Enzymatic ω-oxidation. I. Electron carriers in fatty acid and hydrocarbon hydroxylation. J. Biol. Chem. 1966; 241: 5162
  • Orrenius S., Dallner G., Ernster L. Inhibition of the TPNH-linked lipid peroxidation of liver microsomes by drugs undergoing oxidative demethylation. Biochem. Biophys. Res. Commun. 1964; 14: 329
  • Estabrook R. E., Cooper D. Y., Rosenthal O. The light reversible carbon monoxide inhibition of the steroid C-21 hydroxylase system of the adrenal cortex. Biochem. Z. 1963; 338: 741
  • Kimura T. Redox compounds of adrenal steroid hydroxylase. Biological and Chemical Aspects of Oxygenases, K. Bloch, O. Hayaishi. Maruzen Co., Tokyo 1966
  • Katagiri M., Ganguli B. N., Guhsalus I. C. A. soluble cytochrome P-450 functional in methylene hydroxylation. J. Biol. Chem. 1968; 243: 3543
  • Peterson J. A., Kusunose M., Kusunose E., Coon M. J. Enzymatic ω-oxidation. II. Function of rubrodoxin as the electron carrier in ω-hydroxylation. J. Biol. Chem. 1967; 242: 4334
  • Kusunose M., Ichihara K., Kusunose E., Nozaka J. Oxidation of hydrocarbons in microorganisms. Physiol. Ecol. 1968; 15: 45
  • Kusunose M., Matsumoto J., Ichihara K., Kusunose E., Nozaka J. Requirement of three proteins for hydrocarbon oxidation. J. Biochem. 1967; 61: 665
  • Kusunose M., Ichihara K., Kusunose E., Nozaka J., Matsumoto J. The possible role of flavin on the hydroxylation of hydrocarbon by bacterial enzyme systems. Agr. Biol. Chem. 1967; 31: 990
  • Chang-Ah Y., Gunsalus I. C. Crystalline P-450cam. Biochem. Biophys. Res. Commun. 1970; 40: 1431
  • Yu C. A., Tsibris J. C. M., Hsu M. C. H., Gunsalus I. C. Methylene hydroxylase: Spectral and chemical properties of purified hemoprotein P-450 (CAM) and iron sulfide protein putidaredoxin. Proc. Amer. Oil Chem. Soc. World Congress, Chicago 1970; 161
  • Dus K., Katagiri M., Yu C. A., Erbes D. L., Gunsalus I. C. Chemical characterization of cytochrome P-450 cam. Biochem. Biophys. Res. Commun. 1970; 40: 1423
  • Appleby C. A. A soluble haemoprotein P-450 from nitrogen-fixing bacteroids. Biochem. Biophys. Acta 1967; 147: 399
  • Appleby C. A. Electron transport systems of Rhizobium japonicum. 1. Haemoprotein P-450, other co-reactive pigments, cytochromes and oxidases in bacteroids from N2-fixing root nodules. Biochem. Biophys. Acta 1969; 172: 71
  • Hernandez P. H., Mazel P., Gillette J. R. Studies on the mechanism of mammalian hepatic azoreductase. The effects of phenobarbital and 3-methylcholanthrene on carbon monoxide sensitive and insensitive azoreductase activity. Biochem. Pharmacol. 1967; 16: 1877
  • Lindenmayet A., Smith L. Cytochromes and other pigments of baker's yeast grown aerobically and anaerobically. Biochem. Biophys. Acta 1965; 93: 445
  • Ishidate K., Kawaguchi K., Tagawa K., Hagihara B. Hemoproteins in anaerobically grown yeast cells. J. Biochem. 1969; 65: 375
  • Peterson J. A. Cytochrome content of two pseudomonads containing mixed function oxidase systems. J. Bact. 1970; 103: 714
  • Jurtshuk P., Sekuzu I., Green D. E. Studies on the electron transfer system. LVI. On the formation of an active complex between the apo-D(-)-β-hyroxybutyric dehydrogenase and micellar lecithin. J. Biol. Chem. 1963; 238: 3595
  • Jurtshuk P., Sekuzu I., Green D. E. The interaction of the D(-)-β-hydroxybutyric apoenzyme with lecithin. Biochem. Biophys. Res. Commun. 1961; 6: 76
  • Lee M., Chandler A. C. A study of the nature, growth, and control of bacteria in cutting compounds. J. Bact. 1941; 41: 373
  • Peterson J. A., Coon M. J. Enzymatic ω-oxidation. III. Purification and properties of rubredoxin, a component of the ω-hydroxylation system of Pseudomonas oleovorans. J. Biol. Chem. 1968; 243: 329
  • Lovenberg W., Sobel B. E. Rubredoxin: A new electron transfer protein from Clostridium pasteurianum. Proc. Nat. Acad Sci. U.S.A. 1965; 54: 193
  • Lode E. T., Coon M. J. Enzymatic ω-oxidation. V. Forms of Pseudomonas oleovorans rubredoxin containing one or two iron atoms: Structure and function in ω-hydroxylation. J. Biol. Chem. 1971; 246: 791
  • Shin M., Tagawa K., Arnon D. I. Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts. Biochem. Z. 1963; 338: 84
  • McKenna E. J., Coon M. J. Enzymatic ω-oxidation IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans. J. Biol. Chem. 1970; 245: 3882
  • Peterson J. A., McKenna E. J., Estabrook R. W., Coon M. J. Enzymatic ω-oxidation: Stoichiometry of ω-oxidation of fatty acids. Arch. Biochem. Biophys. 1969; 131: 245
  • Nagai J., Bloch K. Synthesis of oleic acid by Euglena gracilis. J. Biol. Chem. 1965; 240: 3702, (PC)
  • Nagai J., Bloch K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 1966; 241: 1925
  • Nagai J., Bloch K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 1968; 243: 4624
  • Tagawa K., Arnon D. I. Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas. Nature 1962; 195: 537
  • Avron M., Jagendorf A. T. A TPNH diaphorase from chloroplasts. Arch. Biochem. Biophys. 1956; 65: 475
  • Nagai J., Bloch K. Enzymatic desaturation of stearyl ACP. Biological and Chemical Aspects of Oxygenases, K. Bloch, O. Hayaishi. Maruzen Co., Tokyo 1966
  • Fulco A. J., Bloch K. Cofactor requirements for the formation of Δ9-unsaturated fatty acids of Mycobacterium phlei. J. Biol. Chem. 1964; 239: 993
  • Bloomfield D. K., Bloch K. The formation of Δ9-unsaturated fatty acids. J. Biol. Chem. 1960; 235: 337
  • Marsh J. B., James A. T. The conversion of stearic to oleic acid by liver and yeast preparations. Biochim. Biophys. Acta 1962; 60: 320
  • Imai Y. Studies of the lipogenesis in animal tissues under pathological conditions. J. Biochem 1961; 49: 642
  • Gellhorn A., Benjamin W. The intracellular localization of an enzymatic defect of lipid metabolism in diabetic rats. Biochim. Biophys. Acta 1964; 84: 167
  • Sato R. Electron transfer mechanism associated with desaturation of stearyl CoA by liver microsomes. Biological and Chemical Aspects of Oxygenases, K. Bloch, O. Hayaishi. Maruzen Co., Tokyo 1966
  • Omura T., Sato R., Cooper D. Y., Rosenthal O., Estabrook R. W. Function of cytochrome P-450 of microsomes. Fed. Proc. 1965; 24: 1181
  • Strittmatter P. Protein and coenzyme interactions in the NADH-cytochrome b5 reductase system. Fed. Proc. 1965; 24: 1156
  • Conney A. H. Pharmacological implications of microsomal enzyme induction. Pharmacol Rev. 1967; 19: 317
  • Lu A. Y. H., Strobel H. W., Coon M. J. Properties of a solubilized form of cytochrome P-450 containing mixed function oxidase of liver microsomes. Molec. Pharmacol. 1970; 6: 213
  • Omura T., Sanders T., Estabrook R. W., Cooper D. V., Rosenthal O. Isolation from adrenal cortex of a nonheme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P-450 reductase. Arch. Biochem. Biophys. 1966; 117: 660
  • Estabrook R. W., Cohen B. Organization of the microsomal electron transport system. Microsomes and Drug Oxidations, J. R. Gillette, A. H. Conney, G. J. Cosmides, R. W. Estabrook, J. R. Fouts, G. Mannering. Academic Press, N. Y. 1969
  • Siekevitz P. Origin and functional nature of microsomes. Fed. Proc. 1965; 24: 1153
  • Williams C. H., Jr., Kamin H. J. Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. J. Biol. Chem. 1962; 237: 587
  • Phillips A., Langdon R. G. Hepatic triphosphopyridine nucleotide-cytochrome c reductase isolation, characterization, and kinetic studies. J. Biol. Chem. 1962; 237: 2652
  • Masters B. S. S., Kamin H., Gibson Q. H., Williams C. H., Jr. Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 1965; 240: 921
  • Masters B. S. S., Bilimoria M. H., Kamin H., Gibson Q. H. The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 1965; 240: 4081
  • Kamin H., Masters B. S. S., Gibson Q. H., Williams C. H., Jr. Microsomal TPNH-cytochrome c reductase. Fed. Proc. 1965; 24: 1164
  • Kamin H., Masters B. S. S., Gibson Q. H. NADPH-cytochrome c oxidoreductase. Flavins and Flavoproteins, E. C. Slater. Elsevier Publishing Company, Amsterdam 1966
  • Masters B. S. S., Williams C. H., Jr., Kamin H. The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver. Methods of Enzymology, R. W. Estabrook, M. E. Pullman, New York 1967; VoL X
  • Ryan K., Engel L. Hydroxylation of steroids at carbon 21. J. Biol. Chem. 1957; 225: 103
  • Cooper D. Y., Levin S., Narasimhulu S., Rosenthal O., Estabrook R. W. Photochemical action spectrum of the terminal oxidase of mixed function oxidase systems. Science 1965; 147: 400
  • Orrenius S., Gnospelius Y., Das M. L., Ernster L. Structure and Function of the Endoplasmic Reticulum in Animal Cells, F. C. Gran. Academic Press, New York 1967
  • Ziegler D. M., Pettit F. H. Formation of an intermediate N-oxidative demethylation of N,N-dimethylaniline catalyzed by liver microsomes. Biochem. Biophys. Res. Commun. 1964; 15: 188
  • Ziegler D. M., Mitchell C. H., Jollow D. The properties of a purified hepatic microsomal mixed function amine oxidase. Microsomes and Drug Oxidations, J. R. Gillette, R. W. Estabrook, J. R. Fouts, G. Mannering. Academic Press, New York 1969

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