Zimmermann, P. ; Laska, S. ; Kletzin, Arnulf (1999):
Two modes of sulfite oxidation in the extremely thermophilic and acidophilic archaeon acidianus ambivalens.
In: Archives of microbiology, 172 (2), pp. 76-82. ISSN 1432-072X,
[Article]
Abstract
Sulfite-oxidizing enzyme activities were analyzed in cell-free extracts of aerobically grown cells of Acidianus ambivalens, an extremely thermophilic and chemolithoautotrophic archaeon. In the membrane and cytoplasmic fractions, two distinct enzyme activities were found. In the membrane fraction, a sulfite:acceptor oxidoreductase activity was found [530 mU (mg protein)(-1); apparent K(m) for sulfite, 3.6 mM]. In the cytoplasmic fraction the following enzyme activities were found and are indicative of an oxidative adenylylsulfate pathway: adenylylsulfate reductase [138 mU (mg protein)(-1)], adenylylsulfate:phosphate adenyltransferase ["ADP sulfurylase"; 86 mU (mg protein)(-1)], adenylate kinase [650 mU (mg protein)(-1)], and rhodanese [thiosulfate sulfur transferase, 9.2 mU (mg protein)(-1)]. In addition, 5',5"'-P(1),P(4)-di(adenosine-5') tetraphosphate (Ap(4)A) synthase and Ap(4)A pyrophosphohydrolase activities were detected.
| Item Type: | Article |
|---|---|
| Erschienen: | 1999 |
| Creators: | Zimmermann, P. ; Laska, S. ; Kletzin, Arnulf |
| Title: | Two modes of sulfite oxidation in the extremely thermophilic and acidophilic archaeon acidianus ambivalens |
| Language: | English |
| Abstract: | Sulfite-oxidizing enzyme activities were analyzed in cell-free extracts of aerobically grown cells of Acidianus ambivalens, an extremely thermophilic and chemolithoautotrophic archaeon. In the membrane and cytoplasmic fractions, two distinct enzyme activities were found. In the membrane fraction, a sulfite:acceptor oxidoreductase activity was found [530 mU (mg protein)(-1); apparent K(m) for sulfite, 3.6 mM]. In the cytoplasmic fraction the following enzyme activities were found and are indicative of an oxidative adenylylsulfate pathway: adenylylsulfate reductase [138 mU (mg protein)(-1)], adenylylsulfate:phosphate adenyltransferase ["ADP sulfurylase"; 86 mU (mg protein)(-1)], adenylate kinase [650 mU (mg protein)(-1)], and rhodanese [thiosulfate sulfur transferase, 9.2 mU (mg protein)(-1)]. In addition, 5',5"'-P(1),P(4)-di(adenosine-5') tetraphosphate (Ap(4)A) synthase and Ap(4)A pyrophosphohydrolase activities were detected. |
| Journal or Publication Title: | Archives of microbiology |
| Journal volume: | 172 |
| Number: | 2 |
| Divisions: | 10 Department of Biology > Sulfur Biochemistry and Microbial Bioenergetics ?? fb10_mikrobiologie ?? 10 Department of Biology |
| Date Deposited: | 24 May 2011 09:12 |
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