Abstract
Three types of evidence are presented to show that the enzymes that hydroxylate nicotinic acid to 2,6-dihydroxynicotinic acid use water as a source of oxygen atoms. (18)O is incorporated into the products from H(2) (18)O. Molecular oxygen acts as a terminal electron acceptor, one-half molecule being consumed per molecule of hydroxyl groups incorporated. An external electron acceptor is required for activity in purified preparations.
MeSH Terms
Bacillus/enzymology,growth & development,metabolism
Cell-Free System
Chemistry, Organic
Chromatography, DEAE-Cellulose
Culture Media
Electron Transport
Hydroxylation
Mass Spectrometry
Mixed Function Oxygenases/isolation & purification,metabolism
Nicotinic Acids/metabolism
Organic Chemistry Phenomena
Oxygen
Oxygen Consumption
Oxygen Isotopes
Water/metabolism
Chemicals
Culture Media
Nicotinic Acids
Oxygen Isotopes
Water
Mixed Function Oxygenases
Oxygen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hirschberg R
Ensign J C
References (5)
5 references, click to expand
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The hydroxylation of nicotine: the origin of the hydroxyl oxygen.
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PMID: 5879471
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Nicotinic acid metabolism. IV. Ferredoxin-dependent reduction of 6-hydroxynicotinic acid to 6-oxo-1,4,5,6-tetrahydronicotinic acid.
J Biol Chem. 1969 Mar 10;244(5):1204-11
PMID: 5767303
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Nature and mechanisms of oxygenases.
Science. 1969 Apr 25;164(3878):389-96
PMID: 4304952
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THE PATHWAY OF NICOTINIC ACID OXIDATION BY A BACILLUS SPECIES.
J Biol Chem. 1964 Jul;239:2285-91
PMID: 14216418
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Oxidation of nicotinic acid by a Bacillus species: purification and properties of nicotinic acid and 6-hydroxynicotinic acid hydroxylases.
J Bacteriol. 1971 Nov;108(2):751-6
PMID: 5128334