Abstract
The enzymes of a Bacillus species that hydroxylate nicotinic acid to 6-hydroxynicotinic acid and 6-hydroxynicotinic acid to 2,6-dihydroxynicotinic acid were purified and characterized. The purified enzymes contained approximately two molecules of flavine and eight molecules of iron per molecule of enzyme. The enzymes were large (molecular weight, 400,000 to 450,000) and appeared to consist of subunits.
MeSH Terms
Ammonium Sulfate
Bacillus/enzymology,growth & development,metabolism
Cell-Free System
Chemical Precipitation
Chromatography, DEAE-Cellulose
Chromatography, Gel
Culture Media
Electrophoresis
Flavins/analysis
Gels
Hydroxylation
Iron/analysis
Mixed Function Oxygenases/analysis,isolation & purification,metabolism
Molecular Weight
Nicotinic Acids/metabolism
Spectrophotometry
Ultracentrifugation
Chemicals
Culture Media
Flavins
Gels
Nicotinic Acids
Iron
Mixed Function Oxygenases
Ammonium Sulfate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hirschberg R
Ensign J C
References (18)
18 references, click to expand
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