caa a22 4500 477105505 CHVBK 20180405111552.0 cr unu---uuuuu 170330e19961101xx s 000 0 eng 10.1007/BF01574775 doi (NATIONALLICENCE)springer-10.1007/BF01574775 Diverse reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp strain NCIB 9816 [Elektronische Daten] [SM Resnick, K Lee, DT Gibson] Naphthalene dioxygenase (NDO) fromPseudomonas sp strain NCIB 9816 is a multicomponent enzyme system which initiates naphthalene catabolism by catalyzing the addition of both atoms of molecular oxygen and two hydrogen atoms to the substrate to yield enantiomerically pure (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. NDO has a relaxed substrate specificity and catalyzes the dioxygenation of many related 2- and 3-ring aromatic and hydroaromatic (benzocyclic) compounds to their respectivecis-diols. Biotransformations with a diol-accumulating mutant, recombinant strains and purified enzyme components have established that in addition tocis-dihydroxylation, NDO also catalyzes a variety of other oxidations which include monohydroxylation, desaturation (dehydrogenation),O-andN-dealkylation and sulfoxidation reactions. In several cases, the absolute stereochemistry of the oxidation products formed by NDO are opposite to those formed by toluene dioxygenase (TDO). The reactions catalyzed by NDO and other microbial dioxygenases can yield specific hydroxylated compounds which can serve as chiral synthons in the preparation of a variety of compounds of interest to pharmaceutical and specialty chemical industries. We present here recent work documenting the diverse array of oxidation reactions catalyzed by NDO. The trends observed in the oxidation of a series of benzocyclic aromatic compounds are compared to those observed with TDO and provide the basis for prediction of regio- and stereospecificity in the oxidation of related substrates. Based on the types of reactions catalyzed and the biochemical characteristics of NDO, a mechanism for oxygen activation by NDO is proposed. Society for Industrial Microbiology, 1996 asymmetric dihydroxylation nationallicence biocatalysis nationallicence biotransformation nationallicence dealkylation nationallicence desaturation nationallicence dioxygenation nationallicence monooxygenation nationallicence sulfoxidation nationallicence stereospecific oxidation nationallicence Resnick SM The Department of Microbiology, The University of Iowa, 52242, Iowa City, IA, USA aut Lee K. The Department of Microbiology, The University of Iowa, 52242, Iowa City, IA, USA aut Gibson DT The Department of Microbiology, The University of Iowa, 52242, Iowa City, IA, USA aut Journal of Industrial Microbiology Springer-Verlag 17/5-6(1996-11-01), 438-457 0169-4146 17:5-6<438 1996 17 10295 https://doi.org/10.1007/BF01574775 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01574775 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Resnick SM The Department of Microbiology, The University of Iowa, 52242, Iowa City, IA, USA aut NATIONALLICENCE 700 1- Lee K. The Department of Microbiology, The University of Iowa, 52242, Iowa City, IA, USA aut NATIONALLICENCE 700 1- Gibson DT The Department of Microbiology, The University of Iowa, 52242, Iowa City, IA, USA aut NATIONALLICENCE 773 0- Journal of Industrial Microbiology Springer-Verlag 17/5-6(1996-11-01), 438-457 0169-4146 17:5-6<438 1996 17 10295 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer