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Benzylic monooxygenation catalyzed by toluene dioxygenase from Pseudomonas putida

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00404a041· OSTI ID:5410589
Toluene dioxygenase, a multicomponent enzyme system known to oxidize mononuclear aromatic hydrocarbons to cis-dihydrodiols, oxidized indene and indan to 1-indenol and 1-indanol, respectively. In addition, the enzyme catalyzed dioxygen addition to the nonaromatic double bond of indene to form cis-1,2-indandiol. The oxygen atoms in 1-indenol and cis-1,2-indandiol were shown to be derived from molecular oxygen, whereas 70% of the oxygen in 1-indanol was derived from water. All of the isolated products were optically active as demonstrated by /sup 19/F NMR and HPLC discrimination of diastereomeric esters and by chiroptic methods. The high optical purity of (-)-(1R)-indanol (84% enantiomeric excess) and the failure of scavengers of reactive oxygen species to inhibit the monooxygenation reaction supported the contention that monooxygen insertion is mediated by an active-site process. Experiments with 3-(/sup 2/H) indene indicated that equilibration between C-1 and C-3 occurred prior to the formation of the carbon-oxygen bond to yield 1-indenol. Naphthalene dioxygenase also oxidized indan to 1-indanol, which suggested that benzylic monoxygenation may be typical of this group of dioxygenases.
Research Organization:
Univ. of Texas, Austin (USA)
OSTI ID:
5410589
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:4; ISSN BICHA
Country of Publication:
United States
Language:
English