Cell-free extracts of Thiobacillus ferrooxidans grown with thiosulfate
as energy source and prepared at high ammonium sulfate concentrations
and at low ph are capable of polythionate hydrolysis. The enzyme resp
onsible for the hydrolysis of tetrathionate (S4O62-) and pentathionate
(S5O62-) was purified to homogeneity. Enzyme activity during the puri
fication procedure was based on a continuous spectrophotometric method
that detects soluble intermediates that absorb in the UV region. The
end products of hydrolysis of both polythionates by the pure enzyme we
re thiosulfate, sulfur and sulfate. The purified enzyme has a ph optim
um of around 4 and a temperature optimum of 65 degrees C. The activity
is strongly influenced by the presence of sulfate ions. The purified
enzyme is a dimer with two identical subunits of molecular mass 52 kDa
. During purification of tetrathionate hydrolase, fractions able to hy
drolyse trithionate and tetrathionate were separated, indicating that
the two substrates are hydrolysed by different enzymes.