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1.2- dihydroxy naphthalene dioxygenase

Kuhm AE, A Stolz, K-L Ngai, H-J Knackmuss (1991) Purification and characterization of a 1,2-dihydroxy-naphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J Bacteriol 173 3795-3802. [Pg.508]

Regio- and stereospecific oxidation of 9,10-dihydrophenanthrene by naphthalene dioxygenase resulted in (+)-c/5-(35,4i )-3,4-dihydroxy-3,4,9,10-tetrahydrophenanthrene (438, 70% relative yield >95% enantiomeric excess) and (+)-(5)-9-hydroxy-9,10-dihydrophenanthrene (401, 30% relative yield) [189]. [Pg.571]

Figure 13.21 Mononuclear non-haem iron enzymes from each of the five families in structures which are poised for attack by 02. (a) The extradiol-cleaving catechol dioxygenase, 2,3-dihydroxy-biphenyl 1,2-dioxygenase (b) the Rieske dioxygenase, naphthalene 1,2-dioxygenase (c) isopenicillin N-synthase (d) the ot-ketoglutarate dependent enzyme clavaminate synthase and (e) the pterin-dependent phenylalanine hydroxylase. (From Koehntop et al., 2005. With kind permission of Springer Science and Business Media.)... Figure 13.21 Mononuclear non-haem iron enzymes from each of the five families in structures which are poised for attack by 02. (a) The extradiol-cleaving catechol dioxygenase, 2,3-dihydroxy-biphenyl 1,2-dioxygenase (b) the Rieske dioxygenase, naphthalene 1,2-dioxygenase (c) isopenicillin N-synthase (d) the ot-ketoglutarate dependent enzyme clavaminate synthase and (e) the pterin-dependent phenylalanine hydroxylase. (From Koehntop et al., 2005. With kind permission of Springer Science and Business Media.)...

See other pages where 1.2- dihydroxy naphthalene dioxygenase is mentioned: [Pg.105]    [Pg.167]    [Pg.355]    [Pg.505]    [Pg.9]    [Pg.505]    [Pg.463]    [Pg.468]    [Pg.23]    [Pg.2259]    [Pg.2260]    [Pg.593]    [Pg.146]    [Pg.2258]    [Pg.2259]    [Pg.125]    [Pg.91]   
See also in sourсe #XX -- [ Pg.507 ]




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