Studies on the destruction of indole-3-acetic acid by a species of Arthrobacter II. Properties of the oxidation system

1. Some properties of the IAA-oxidizing activity of lyophilizedcells of Artkrobacter sp. were examined.
2. 1. IAA oxidationseems not to be catalysed by peroxidase, polyphenoloxidase,laccase or dehydrogenase, but by an oxidase systemdifferentfrom the one reported earlier.
3. 2. The optimal pH for the oxidizingsystem is ca. 6.0, and thesystem is comparatively stable atpH 5 to 10.
4. 3. The optimal substrate (IAA) level is 10^–3M.
5. 4. Activity is inhibited by metal-chelating reagents, suchassodium azide, potassium cyanide, sodium diethyldithiocarbamate,potassium xanthogenate and 8-hydroxyquinoline, and sulfhydrylreagents, such as iodoacetamide, monofluoroacetic acid, p-chloromercuribenzoate,isatin, ß-naphthoquinone and ß-naphthoquinone-4-sulfonate.Hydroxybenzoic acid, sulfosalicylic acid and 2,4-dichlorophenolare also inhibitory.
6. 5. None of the IAA analogs tested (indole,skatole, 2,3-dihydroxyindole,indole-3-aldehyde, -3-carboxylicacid, -3-propionic acid, -3-lacticacid, -3-butyric acid, 5-hydroxyindole-3-aceticacid and D,L-tryptophan) are oxidized by the cells, and someanalogs (indole-3-carboxylicacid, -3-propionic acid, -3-butyricacid, 5-hydroxyindole-3-aceticacid, naphthalene-acetic acidand 2,4-D) are inhibitory at comparativelyhigh concentrations.
7. 6. The oxidizing activity is not stimulated by Mn⁺⁺ and isinhibitedby Co⁺⁺, Cu⁺⁺ and Hg⁺⁺.
8. 7. The oxidizing activitydisappears completely within 6 hrat 30, but is kept unchangedat least for two weeks at –20.

(Received August 7, 1967; )