Inhibition of diethyl ether degradation in Rhodococcus sp. strain DEE5151 by glutaraldehyde and ethyl vinyl ether.

[1]  Yong-Hak Kim,et al.  Degradation of Alkyl Ethers, Aralkyl Ethers, and Dibenzyl Ether by Rhodococcus sp. Strain DEE5151, Isolated from Diethyl Ether-Containing Enrichment Cultures , 2004, Applied and Environmental Microbiology.

[2]  M. Watwood,et al.  Limitations of the lignin peroxidase system of the white-rot fungus, Phanerochaete chrysosporium , 1996, Applied Microbiology and Biotechnology.

[3]  D. Gibson,et al.  Biotransformation of anisole and phenetole by aerobic hydrocarbonoxidizing bacteria , 1993, Biodegradation.

[4]  C. Cerniglia,et al.  Two polycyclic aromatic hydrocarbon o-quinone reductases from a pyrene-degrading Mycobacterium. , 2003, Archives of Biochemistry and Biophysics.

[5]  Spencer S Ericksen,et al.  Characterization of substrate binding to cytochrome P450 1A1 using molecular modeling and kinetic analyses: case of residue 382. , 2003, Drug metabolism and disposition: the biological fate of chemicals.

[6]  N. Turner,et al.  Identification of a New Class of Cytochrome P450 from a Rhodococcus sp , 2002, Journal of bacteriology.

[7]  J. Vandecasteele,et al.  Microbial degradation and fate in the environment of methyl tert-butyl ether and related fuel oxygenates , 2001, Applied Microbiology and Biotechnology.

[8]  G. Miller,et al.  Binding and oxidation of alkyl 4-nitrophenyl ethers by rabbit cytochrome P450 1A2: evidence for two binding sites. , 2001, Biochemistry.

[9]  Sandra N. Mohr,et al.  Human cytochrome P450 isozymes in metabolism and health effects of gasoline ethers. , 2001, Research report.

[10]  L. Alvarez-Cohen,et al.  Substrate interactions in BTEX and MTBE mixtures by an MTBE-degrading isolate. , 2001, Environmental science & technology.

[11]  S. Miyoshi,et al.  Purification and characterization of 2-ethoxyphenol-induced cytochrome P450 from Corynebacterium sp. strain EP1. , 1999, Canadian journal of microbiology.

[12]  F. Gonzalez,et al.  Metabolism of methyl tert-butyl ether and other gasoline ethers in mouse liver microsomes lacking cytochrome P450 2E1. , 1999, Toxicology letters.

[13]  C. Condee,et al.  Biodegradation of the gasoline oxygenates methyl tert-butyl ether, ethyl tert-butyl ether, and tert-amyl methyl ether by propane-oxidizing bacteria , 1997, Applied and environmental microbiology.

[14]  L. Ciuffetti,et al.  Metabolism of Diethyl Ether and Cometabolism of Methyl tert-Butyl Ether by a Filamentous Fungus, a Graphium sp , 1997, Applied and environmental microbiology.

[15]  L. Newman,et al.  Toluene 2-Monooxygenase-Dependent Growth of Burkholderia cepacia G4/PR1 on Diethyl Ether , 1997, Applied and environmental microbiology.

[16]  C. Kulpa,et al.  Biodegradation of methyl t-butyl ether by pure bacterial cultures , 1997, Applied Microbiology and Biotechnology.

[17]  N. Russell,et al.  Bacterial scission of ether bonds. , 1996, Microbiological reviews.

[18]  J. Ahokas,et al.  Inhibition of P-450 by aucubin: is the biological activity of aucubin due to its glutaraldehyde-like aglycone? , 1995, Toxicology letters.

[19]  J. Halpert,et al.  Escherichia coli expression of site-directed mutants of cytochrome P450 2B1 from six substrate recognition sites: substrate specificity and inhibitor selectivity studies. , 1995, Chemical research in toxicology.

[20]  D. Arp,et al.  Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea , 1994, Applied and environmental microbiology.

[21]  R. Mayer,et al.  Use of 7-alkoxyphenoxazones, 7-alkoxycoumarins and 7-alkoxyquinolines as fluorescent substrates for rainbow trout hepatic microsomes after treatment with various inducers. , 1994, Biochemical pharmacology.

[22]  K. Timmis,et al.  Purification and characterization of cytochrome P450RR1 from Rhodococcus rhodochrous. , 1993, European journal of biochemistry.

[23]  K. Timmis,et al.  Two independently regulated cytochromes P-450 in a Rhodococcus rhodochrous strain that degrades 2-ethoxyphenol and 4-methoxybenzoate , 1993, Journal of bacteriology.

[24]  N. Boens,et al.  Interaction of 7-n-alkoxycoumarins with cytochrome P-450(2) and their partitioning into liposomal membranes. Assessment of methods for determination of membrane partition coefficients. , 1992, The Biochemical journal.

[25]  B. Kalyanaraman,et al.  Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes. , 1990, The Biochemical journal.

[26]  M. Isobe,et al.  Comparative studies on the metabolism and mutagenicity of vinyl ethers. , 1989, Journal of pharmacobio-dynamics.

[27]  T. Umezawa,et al.  Cleavages of aromatic ring and β‐O‐4 bond of synthetic lignin (DHP) by lignin peroxidase , 1989, FEBS letters.

[28]  A. E. Greenberg,et al.  Standard methods for the examination of water and wastewater : supplement to the sixteenth edition , 1988 .

[29]  A. Trautwein,et al.  4-Methoxybenzoate monooxygenase from Pseudomonas putida: isolation, biochemical properties, substrate specificity, and reaction mechanisms of the enzyme components. , 1988, Methods in enzymology.

[30]  R. Farrell,et al.  Enzymatic "combustion": the microbial degradation of lignin. , 1987, Annual review of microbiology.

[31]  R. Crawford,et al.  Transformations of arylpropane lignin model compounds by a lignin peroxidase of the white-rot fungus Phanerochaete chrysosporium. , 1986, Archives of biochemistry and biophysics.

[32]  E. Arnold,et al.  Standard methods for the examination of water and wastewater. 16th ed. , 1985 .

[33]  S. Kirkeby,et al.  The effect of fixation on esterases. , 1984, Acta histochemica.

[34]  R. Mayer,et al.  Differential effects of phenobarbitone and 3-methylcholanthrene induction on the hepatic microsomal metabolism and cytochrome P-450-binding of phenoxazone and a homologous series of its n-alkyl ethers (alkoxyresorufins). , 1983, Chemico-biological interactions.

[35]  L. Kochoumian,et al.  A comparison of different enzyme-antibody conjugates for enzyme-linked immunosorbent assay. , 1979, Journal of immunological methods.