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Autor(en): Trenz, Stefan Peter
Engesser, Karl-Heinrich
Fischer, Peter
Knackmuss, Hans-Joachim
Titel: Degradation of fluorene by Brevibacterium sp. strain DPO 1361: a novel C-C bond cleavage mechanism via 1,10-dihydro-1,10-dihydroxyfluoren-9-one
Erscheinungsdatum: 1994
Dokumentart: Zeitschriftenartikel
Erschienen in: Journal of bacteriology 176 (1994), S. 789-795. URL http://jb.asm.org/content/176/3/789
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-75802
http://elib.uni-stuttgart.de/handle/11682/2015
http://dx.doi.org/10.18419/opus-1998
Zusammenfassung: Angular dioxygenation has been established as the crucial step in dibenzofuran degradation by Brevibacterium sp. strain DPO 1361 (V. Strubel, K. H. Engesser, P. Fischer, and H.-J. Knackmuss, J. Bacteriol. 173:1932-1937, 1991). The same strain utilizes biphenyl and fluorene as sole sources of carbon and energy. The fluorene degradation sequence is proposed to be initiated by oxidation of the fluorene methylene group to 9-fluorenol. Cells grown on fluorene exhibit pronounced 9-fluorenol dehydrogenase activity. Angular dioxygenation of the 9-fluorenone thus formed yields 1,10-dihydro-1,10-dihydroxyfluoren-9-one (DDF). A mechanistic model is presented for the subsequent C-C bond cleavage by an NAD(+)-dependent DDF dehydrogenase, acting on the angular dihydrodiol. This enzyme was purified and characterized as a tetramer of four identical 40-kDa subunits. The following Km values were determined: 13 microM for DDF and 65 microM for 2,3-dihydro-2,3-dihydroxybiphenyl. The enzyme also catalyzes the production of 3-(2'-carboxyphenyl)catechol, which was isolated, and structurally characterized, in the form of the corresponding lactone, 4-hydroxydibenzo-(b,d)-pyran-6-one. Stoichiometry analysis unequivocally demonstrates that angular dioxygenation constitutes the principal pathway in Brevibacterium sp. strain DPO 1361.
Enthalten in den Sammlungen:04 Fakultät Energie-, Verfahrens- und Biotechnik

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