2and 4-acetoxy derivatives, preferentially the 4compound,1a-el except for acetoxylation with Pd(OAc)2 which gives the 3-acetoxybipheny1.1f) Biphenyl is normally metabolized by hydroxylation to either the 2-, 4-, or both, hydroxylated derivatives. It was reported, however, that young rats hydroxylate biphenyl to both the 2and 4-hydroxy compounds whereas adult rats preferentially form the 4-hydro...

Mutants were produced in the A-domain of HbpR, a protein belonging to the XylR family of σ(54)-dependent transcription activators, with the purpose of changing its effector recognition specificity from 2-hydroxybiphenyl (2-HBP, the cognate effector) to 2-chlorobiphenyl (2-CBP). Mutations were introduced in the hbpR gene part for the A-domain via error-prone polymerase chain reaction, and assemb...

rhodococcus fmf is a gram-positive bacterium isolated for the first time from soil samples of tabriz refinery in iran. this microorganism is able to catabolize dibenzothiophene to 2-hydroxybiphenyl and inorganic sulfur without the destruction of carbon-carbon bonds. three structural genes, dsza, dszb, and dszc have been characterized and shown to be responsible for this phenotype. in this work,...

Pseudomonas azelaica HBP1 is one of the few bacteria known to completely mineralize the biocide and toxic compound 2-hydroxybiphenyl (2-HBP), but the mechanisms of its tolerance to the toxicity are unknown. By transposon mutant analysis and screening for absence of growth on water saturating concentrations of 2-HBP (2.7 mM) we preferentially found insertions in three genes with high homology to...

Pseudomonas azelaica HBP1 can use 2-hydroxybiphenyl (2-HBP) and 2,2'-dihydroxybiphenyl as sole carbon and energy sources by means of the hbp regulon. This regulon is composed of three genes, hbpCA and hbpD, coding for enzymes of a meta-cleavage pathway and the hbpR gene, which codes for a XylR/DmpR-type transcription regulator. It was previously shown that HbpR activates transcription from two ...

Rhodococcus FMF is a gram-positive bacterium isolated for the first time from soil samples of Tabriz refinery in Iran. This microorganism is able to catabolize dibenzothiophene to 2-hydroxybiphenyl and inorganic sulfur without the destruction of carbon-carbon bonds. Three structural genes, dszA, dszB, and dszC have been characterized and shown to be responsible for this phenotype. In this work,...

Gasoline-contaminated soil from Isfahan, Iran was selected to isolate a bacterium capable of desulfurizing dibenzothiophene (DBT). The isolated strain was named R1 and identified as Rhodococcus erythropolis through biochemical tests as well as sequencing of 16S rRNA gene. This strain could efficiently produce 2-hydroxybiphenyl (HBP) from DBT via the 4S metabolic pathway. The highest HBP amount ...

Out of 17 samples collected from diverse environments, 110 bacterial isolates of varied characteristics were screened for their dibenzothiophene-desulphurizing activity. A single isolate, Eu-32, originating from a soil sample taken from the roots of a eucalyptus tree, displayed dibenzothiophene-desulphurizing activity. This isolate metabolized dibenzothiophene to 2-hydroxybiphenyl (2-HBP), as d...

Dibenzothiophene (DBT) and their derivatives, accounting for the major part of the sulfur components in crude oil, make one of the most significant pollution sources. The DBT sulfone monooxygenase BdsA, one of the key enzymes in the "4S" desulfurization pathway, catalyzes the oxidation of DBT sulfone to 2'-hydroxybiphenyl 2-sulfonic acid (HBPSi). Here, we determined the crystal structure of Bds...