Degradation of 2-hydroxybiphenyl and 2,2 prime -dihydroxybiphenyl by Pseudomonas sp. strain HBP1
- Univ. of California, Riverside (USA)
Pseudomonas sp. strain HBP1 was found to grow on 2-hydroxy- and 2,2{prime}-dihydroxy-biphenyl as the sole carbon and energy sources. The first step in the degradation of these compounds was catalyzed by an NADH-dependent monooxygenase. The enzyme inserted a hydroxyl group adjacent to the already existing hydroxyl group to form 2,3-dihydroxybiphenyl when acting on 2-hydroxybiphenyl and to form 2,2{prime},3-trihydroxybiphenyl when acting on 2,2{prime}-dihydroxybiphenyl. To be substrates of the monooxygenase, compounds required a 2-hydroxyphenyl-R structure, with R being a hydrophobic group (e.g., methyl, ethyl, propyl, sec-butyl, phenyl, or 2-hydroxyphenyl). Several chlorinated hydroxybiphenyls served as pseudosubstrates by effecting consumption of NADH and oxygen without being hydroxylated. Further degradation of 2,3-dihydroxy- and 2,2{prime},3-trihydroxybiphenyl involved meta cleavage, with subsequent formation of benzoate and salicylate, respectively.
- OSTI ID:
- 5086877
- Journal Information:
- Applied and Environmental Microbiology; (USA), Journal Name: Applied and Environmental Microbiology; (USA) Vol. 54:11; ISSN 0099-2240; ISSN AEMID
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
540220* -- Environment
Terrestrial-- Chemicals Monitoring & Transport-- (1990-)
AROMATICS
BACTERIA
BIODEGRADATION
BIOLOGICAL PATHWAYS
BIPHENYL
CHEMICAL REACTIONS
COENZYMES
DECOMPOSITION
ENZYME ACTIVITY
ENZYMES
GROWTH
HYDROCARBONS
HYDROXY COMPOUNDS
METABOLISM
MICROORGANISMS
NADH2
NUCLEOTIDES
ORGANIC COMPOUNDS
OXIDOREDUCTASES
OXYGENASES
PSEUDOMONAS