Publication Date:
2016-01-21
Description:
The mechanism of sulfate assimilation was investigated in Rhodopseudomonas sulfidophila, a bacterium able to grow either photoautotrophically, with sulfide as electron donor, or photoheterotrophically with sulfate as sole sulfur source. ATP sulfurylase, adenosine-5′-phosphosulfate kinase, 3′-phosphoadenosine-5′-phosphosulfate sulfotransferase, thiosulfonate reductase and cysteine synthase were present. Reduced sulfur compounds, especially sulfide and sulfite repressed all steps of sulfate activation and reduction including sulfate uptake. Adenosine-5′-phosphosulfate kinase activity in contrast to the other activities was high in the presence of cysteine or reduced glutathione in the growth medium. Sulfur was incorporated into the cellular sulfolipid from sulfate and also from reduced sulfur compounds like cysteine and thiosulfate. The activity of 3′-phosphoadenosine-5′-phosphosulfate sulfotransferase was rapidly lost during gel filtration or dialysis. From comparison with other sulfotransferases and from the specific cofactor requirement for the enzyme of R. sulfidophila it is concluded that two different low molecular weight cofactors are required in this system. A reaction sequence is proposed involving thioredoxin as the reductant of another dialysable low molecular weight cofactor, that binds to the protein.
Type:
Article
,
PeerReviewed
Format:
text
Permalink
