Microbial Oxidation of Naphthalene to cis-1,2-Naphthalene Dihydrodiol Using Naphthalene Dioxygenase in Biphasic Media
نویسندگان
چکیده
منابع مشابه
Microbial oxidation of naphthalene. I. Factors concerning salicylate accumulation.
Little information has been contributed to the mechanisms of biological degradation of polycyclic hydrocarbons. The oxidation of naphthalene has received the most attention. Strawinski and Stone (1943, 1954) reported the isolation of substantial amounts of salicylic acid ("most" of the 2.9 mg per ml medium of ether extractable product) from the breakdown of naphthalene by Pseudomonas aeruginosa...
متن کاملAldose reductase catalyzes the oxidation of naphthalene-1, 2-dihydrodiol for the formation of ortho-naphthoquinone.
The oxidation of naphthalene-1,2-dihydrodiol (ND) to o-naphthoquinone (NQ) in the lens is believed to be responsible for the formation of cataracts in naphthalene-fed rats. Studies using either recombinant rat lens (RLAR) or human muscle aldose reductase (HMAR) incubated in vitro with ND in the presence of NAD(P) verified that aldose reductase (EC 1.1.1.21) is the dihydrodiol dehydrogenase that...
متن کاملPlasmid gene organization: naphthalene/salicylate oxidation.
Genes for naphthalene metabolism are localized on nah7, an 83-kilobase (kb) plasmid, in two gene clusters under salicylate control. Polar mutations formed by insertion of the transposon Tn5 permit detection of the transcription direction and the gene organization within two approximately 10-kb DNA segments separated by a approximately 7-kb regulatory gene region. The gene cluster specifying con...
متن کاملStructure and increased thermostability of Rhodococcus sp. naphthalene 1,2-dioxygenase.
Rieske nonheme iron oxygenases form a large class of aromatic ring-hydroxylating dioxygenases found in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth, making them good candidates for use in synthesis of chiral intermediates and bioremediation. Studies of the chemical stability and thermostability of these enzymes thus b...
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ژورنال
عنوان ژورنال: Biotechnology Progress
سال: 2008
ISSN: 8756-7938
DOI: 10.1021/bp070416h