Affiliation:
1. Division of Plant Industry, C.S.I.R.O., Canberra, Australia
Abstract
Two heterotrophic bacteria that oxidized thiosulfate to tetrathionate were isolated from soil. The enzyme system in one of the isolates (C-3) was constitutive, but in the other isolate (A-50) it was induced by thiosulfate or tetrathionate. The apparent
K
m
for oxygen for thiosulfate oxidation by A-50 was about 223 μ
m
, but, for lactate oxidation by A-50 or thiosulfate oxidation by C-3, the apparent
K
m
for oxygen was below 2 m
m
. The oxidation of thiosulfate by A-50 was first order with respect to oxygen from 230 μ
m
. The rate of oxidation was greatest at
p
H 6.3 to 6.8 and at about 10 m
m
thiosulfate, and it was strongly inhibited by several metal-binding reagents. Extracts of induced A-50 reduced ferricyanide, endogenous cytochrome
c
, and mammalian cytochrome
c
in the presence of thiosulfate. A-50, once induced to oxidize thiosulfate, also reduced tetrathionate to thiosulfate in the presence of an electron donor such as lactate. The optimal
p
H for this reaction was at 8.5 to 9.5, and the reaction was first order with respect to tetrathionate. There was no correlation between the formation of the thiosulfate-oxidizing enzyme of A-50 and the incorporation of thiosulfate-sulfur into cell sulfur. Thiosulfate did not affect the growth rate or yield of A-50.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
69 articles.
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