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Toluene/o-xylene monooxygenase

Toluene/o-xylene monooxygenase in P. stutzeri strain 0X1 carried ont snccessive monooxygenation of o-xylene (Bertoni et al. 1998), and the tolnene-4-monooxygenase of Pseudomonas mendocina KRl and tolnene-3-monooxygenase of Ralstonia pickettii PKOl can hydroxylate benzene, tolnene, and o-xylene (Tao et al. 2004 Vardar and Wood 2004). [Pg.108]

Bertoni G, M Martino, E Galli, P Barbieri (1998) Analysis of the gene cluster encoding toluene/o-xylene monooxygenase from Pseudomonas stutzeri 0X1. Appl Environ Microbiol 64 3626-3632. [Pg.136]

Vardar G, TK Wood (2004) Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzeri 0X1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol. Appl Environ Microbiol 70 3253-3262. [Pg.146]

Ryoo D, Shim H, Canada K, Barbieri P, Wood TK (2000) Aerobic degradation of tetra-chloroethylene by toluene-o-xylene monooxygenase of Pseudomonas stutzeri OX1. Nat Biotechnol 18 775-778... [Pg.61]

Figure 12. Active site structure of toluene/o-xylene monooxygenase (ToMOH) from Pseudomonas stutzeri 0X1 (A) fully oxidized native ToMOH (PDB code 2INC), (B) Mn /Mn ToMOH (PDB code 2IND), and (C) reduced ToMOH-azide complex (PDB code ITOR). Figure 12. Active site structure of toluene/o-xylene monooxygenase (ToMOH) from Pseudomonas stutzeri 0X1 (A) fully oxidized native ToMOH (PDB code 2INC), (B) Mn /Mn ToMOH (PDB code 2IND), and (C) reduced ToMOH-azide complex (PDB code ITOR).
Figure 13. EPR spectra of the Fe -Fe" -W intermediate generated in the reaction of reduced mow mutant of toluene/o-xylene monooxygenase with dioxygen. Reprinted with permission from [214]. Copyright 2006, American Chemical Society. Figure 13. EPR spectra of the Fe -Fe" -W intermediate generated in the reaction of reduced mow mutant of toluene/o-xylene monooxygenase with dioxygen. Reprinted with permission from [214]. Copyright 2006, American Chemical Society.
Cafaro V, Scognamiglio R, Viggiani A, Izzo V, Passaro I, Notomista E, Dal Piaz F, Amoresano A, Casbarra A, Pucci P, Di Donato A. 2002. Expression and purification of the recombinant subunits of toluene/o-xylene monooxygenase and reconstitution of the active complex. Eur JBiochem 269 5689-5699. [Pg.369]

Sazinsky MH, Bard J, Di Donato A, Lippard SJ. 2004. Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri 0X1 insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases. JBiol Chem 279 30600-30610. [Pg.369]

Rudd DJ, Sazinsky MH, Lippard SJ, Hedman B, Hodgson KO. 2005. X-ray, absorption spectroscopic study of the reduced hydroxylases of methane monooxygenase and toluene/o-xylene monooxygenase differences in active site structure and effects of the coupling proteins MMOB and ToMOD. Inorg Chem 44 4546-4554. [Pg.369]

McCormick MS, Sazinsky MH, Condon KL, Lippard SJ. 2006. X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior. J Am Chem Soc 128 15108-15110. [Pg.369]

Murray LJ, Garcia-Serres R, Naik S, Huynh BH, Lippard SJ. 2006. Dioxygen activation at non-heme diiron centers characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase. JAm Chem Soc 128 7458-7459. [Pg.369]

Toluene/o-xylene (ToMO) from P. stutzeri 0X1, which has recently been expressed and purified, belongs to a class of bacterial multicomponent monooxygenases, and is also closely related to MMO [11,12,207]. It catalyzes the oxidation... [Pg.300]


See other pages where Toluene/o-xylene monooxygenase is mentioned: [Pg.300]    [Pg.74]    [Pg.300]    [Pg.74]    [Pg.126]   
See also in sourсe #XX -- [ Pg.300 , Pg.301 , Pg.302 ]




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