Anaerobic degradation ofm-cresol via methyl oxidation to 3-hydroxybenzoate by a denitrifying bacterium

1995 ◽  
Vol 164 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Cornelus F. C. Bonting ◽  
Sabine Schneider ◽  
Günther Schmidtberg ◽  
Georg Fuchs
2019 ◽  
Vol 25 (18) ◽  
pp. 4722-4731 ◽  
Author(s):  
Julian Küppers ◽  
Patrick Becker ◽  
René Jarling ◽  
Marvin Dörries ◽  
Nevenka Cakić ◽  
...  

1999 ◽  
Vol 171 (4) ◽  
pp. 230-236 ◽  
Author(s):  
M. M. Häggblom ◽  
L. Y. Young

2011 ◽  
Vol 78 (5) ◽  
pp. 1606-1610 ◽  
Author(s):  
Sven Lahme ◽  
Jens Harder ◽  
Ralf Rabus

ABSTRACTA novel alphaproteobacterium isolated from freshwater sediments, strain pMbN1, degrades 4-methylbenzoate to CO2under nitrate-reducing conditions. While strain pMbN1 utilizes several benzoate derivatives and other polar aromatic compounds, it cannot degradep-xylene or other hydrocarbons. Based on 16S rRNA gene sequence analysis, strain pMbN1 is affiliated with the genusMagnetospirillum.


2002 ◽  
Vol 177 (3) ◽  
pp. 235-243 ◽  
Author(s):  
Heinz Wilkes ◽  
Ralf Rabus ◽  
Thomas Fischer ◽  
Antje Armstroff ◽  
Astrid Behrends ◽  
...  

1990 ◽  
Vol 1 (4) ◽  
pp. 243-251 ◽  
Author(s):  
Harald Platen ◽  
Bernhard Schink

2004 ◽  
Vol 181 (3) ◽  
pp. 182-194 ◽  
Author(s):  
Michael Kube ◽  
Johann Heider ◽  
Judith Amann ◽  
Peter Hufnagel ◽  
Simon K�hner ◽  
...  

1998 ◽  
Vol 180 (14) ◽  
pp. 3644-3649 ◽  
Author(s):  
Bodo Philipp ◽  
Bernhard Schink

ABSTRACT The denitrifying bacterium Azoarcus anaerobius LuFRes1 grows anaerobically with resorcinol (1,3-dihydroxybenzene) as the sole source of carbon and energy. The anaerobic degradation of this compound was investigated in cell extracts. Resorcinol reductase, the key enzyme for resorcinol catabolism in fermenting bacteria, was not present in this organism. Instead, resorcinol was hydroxylated to hydroxyhydroquinone (HHQ; 1,2,4-trihydroxybenzene) with nitrate or K3Fe(CN)6 as the electron acceptor. HHQ was further oxidized with nitrate to 2-hydroxy-1,4-benzoquinone as identified by high-pressure liquid chromatography, UV/visible light spectroscopy, and mass spectroscopy. Average specific activities were 60 mU mg of protein−1 for resorcinol hydroxylation and 150 mU mg of protein−1 for HHQ dehydrogenation. Both activities were found nearly exclusively in the membrane fraction and were only barely detectable in extracts of cells grown with benzoate, indicating that both reactions were specific for resorcinol degradation. These findings suggest a new strategy of anaerobic degradation of aromatic compounds involving oxidative steps for destabilization of the aromatic ring, different from the reductive dearomatization mechanisms described so far.


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