The hydroxylation of nicotine: The origin of the hydroxyl oxygen

Hochstein, Lawrence I.; Dalton, Bonnie P.

doi:10.1016/0006-291x(65)90535-8

Cited by 24 publications

(8 citation statements)

References 6 publications

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“…Similar observations have been reported for the hydroxylation of picolinic acid by Rhodotorula MR (Dagley & Johnson, 1963) and the hydroxylation of nicotine by Arthrobacter oxydans (Hochstein & Dalton, 1965.…”

Section: Discussionsupporting

confidence: 88%

“…The resulting obligatory requirement for an electron acceptor may be satisfied by Methylene Blue, Nitro Blue Tetrazolium or the membrane fraction from 2-furoate-grown cells. Other hydroxylases utilizing oxygen from water all catalyse the initial reactions in the bacterial degradation of pyridine-ring compounds and all display an electron-acceptor requirement (Hunt et al, 1958;Dagley & Johnson, 1963;Hochstein & Dalton, 1965;Hayaishi, 1969;Hirschberg & Ensign, 1971a,b).…”

Section: Glutaratementioning

confidence: 99%

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Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2

Kitcher

Trudgill

Rees

1972

Biochemical Journal

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1. 2-Furoyl-CoA hydroxylase of Pseudomonas putida F2 has been purified 60-fold by a combination of (NH(4))(2)SO(4) fractionation, DEAE-cellulose chromatography and agarose chromatography. 2. The purified enzyme catalyses the formation of 5-hydroxy-2-furoyl-CoA, which tautomerizes to form 5-oxo-Delta(2)-dihydro-2-furoyl-CoA. 3. The enzyme has a requirement for an electron acceptor that can be satisfied by a membrane preparation from 2-furoate-grown Ps. putida F2 or by artificial electron acceptors, and so presumably the incorporated oxygen atom is derived from water rather than molecular oxygen. 4. The enzyme is a large protein with a molecular weight of 3.27x10(6) and is disrupted to form inactive subunits in the presence of 0.2% (w/v) sodium dodecyl sulphate. It has a pH optimum of 8.5-9.5, a K(m) for 2-furoyl-CoA of 20.2mum and an absorption spectrum with a trough at 265nm and a single peak at 273nm. No absorption peaks are detectable in the visible region of the spectrum. 5. The enzyme is resistant to the effects of a wide range of potential inhibitors, but is inhibited by the copper-chelating agents bathocuproin and cuprizone, though not by sodium diethyldithiocarbamate. 6. Flavins are absent and the iron content does not show a sustained increase during purification. The copper content of the protein increases in close correlation with the increase in specific activity during purification. 7. A catalytic sequence for the hydroxylation of 2-furoyl-CoA by a copper protein is proposed.

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Section: Discussionsupporting

confidence: 88%

Section: Glutaratementioning

confidence: 99%

Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2

Kitcher

Trudgill

Rees

1972

Biochemical Journal

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“…Without an addition of molybdate to the growth medium the absorbances reached were at least 10-fold lower than in the presence of 10 -8 M molybdate (Fig. A. oxidans P-34 was so far routinely grown in the presence of 0.1% yeast extract [3], whereas another strain (DSM 420) was cultured in the presence of 0.05% yeast extract [2]. The consumption of nicotine during growth also depended on the presence of molybdate (Fig.…”

Section: Resultsmentioning

confidence: 98%

Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase

Freudenberg

1988

FEMS Microbiology Letters

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“…Hydroxylation of pyridine derivatives such as nicotine (Hochstein & Dalton, 1965) and nicotinic acid (Hunt et al, 1958) by enzymes obtained from micro-organisms occurs from water rather than from molecular 02 as found with the model system and microbial hydroxylations of substituted homocyclic compounds. Hayaishi (1969) suggested that this type of hydroxylation, which was also known to occur in the hydroxylation of purines and pyrimidines, took place preferably with hydrophilic substrates.…”

Section: Discussionmentioning

confidence: 93%

Microbial metabolism of the pyridine ring. Formation of pyridinediols (dihydroxypyridines) as intermediates in the degradation of pyridine compounds by micro-organisms

Houghton

Cain

1972

Biochemical Journal

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1. Several species of micro-organisms that were capable of utilizing pyridine compounds as carbon and energy source were isolated from soil and sewage. Compounds degraded included pyridine and the three isomeric hydroxypyridines. 2. Suitable modifications of the cultural conditions led to the accumulation of pyridinediols (dihydroxypyridines), which were isolated and characterized. 3. Three species of Achromobacter produced pyridine-2,5-diol from 2- or 3-hydroxypyridine whereas an uncommon Agrobacterium sp. (N.C.I.B. 10413) produced pyridine-3,4-diol from 4-hydroxypyridine. 4. On the basis of chemical isolation, induction of the necessary enzymes in washed suspensions and the substrate specificity exhibited by the isolated bacteria, the initial transformations proposed are: 2-hydroxypyridine --> pyridine-2,5-diol; 3-hydroxypyridine --> pyridine-2,5-diol and 4-hydroxypyridine --> pyridine-3,4-diol. 5. A selected pyridine-utilizer, Nocardia Z1, did not produce any detectable hydroxy derivative from pyridine, but carried out a slow oxidation of 3-hydroxypyridine to pyridine-2,3-diol and pyridine-3,4-diol. These diols were not further metabolized. 6. Addition of the isomeric hydroxypyridines to a model hydroxylating system resulted in the formation of those diols predicted by theory.

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The hydroxylation of nicotine: The origin of the hydroxyl oxygen

Cited by 24 publications

References 6 publications

Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2

Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2

Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase

Microbial metabolism of the pyridine ring. Formation of pyridinediols (dihydroxypyridines) as intermediates in the degradation of pyridine compounds by micro-organisms

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