Fritz, Günter and Buechert, Thomas and Huber, Harald and Stetter, Karl O. and Kroneck, Peter M. H. (2000) Adenylylsulfate reductases from archaea and bacteria are 1 : 1 alpha beta-heterodimeric iron-sulfur flavoenzymes - high similarity of molecular properties emphasizes their central role in sulfur metabolism. FEBS LETTERS, 473 (1). pp. 63-66. ISSN 0014-5793
Full text not available from this repository. (Request a copy)Abstract
Highly active adenylylsulfate (APS) reductase was isolated under N-2/H-2 from sulfate-reducing and sulfide-oxidizing bacteria and archaea, It tvas a I:I alpha beta-heterodimer of molecular mass approximate to 95 kDa, and two subunits (alpha approximate to 75, beta approximate to 20 kDa), The specific activity was 11-14 mu mol (min mg)(-1); cofactor analysis revealed 0.96 +/- 0.05 FAD, 7.5 +/- 0.1 Fe and 7.9 +/- 0.25 S2-. The photochemically reduced enzyme had a multiline EPR spectrum resulting from two interacting [4Fe-4S] centers. The properties of the different APS reductases were remarkably similar, although the enzyme is involved in different metabolic pathways and was isolated from phylogenetically far separated organisms. A structural model is proposed, with FAD bound to the alpha-subunit, and two [4FE-4S] centers located in close proximity on the beta-subunit. (C) 2000 Federation of European Biochemical Societies.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SULFATE-REDUCING BACTERIA; DESULFOVIBRIO-VULGARIS HILDENBOROUGH; DISSIMILATORY SULFITE REDUCTASE; NITROUS-OXIDE REDUCTASE; THIOBACILLUS-DENITRIFICANS; ARCHAEOGLOBUS-FULGIDUS; ENZYME; GENES; DESULFORUBIDIN; FLAVOPROTEINS; adenylylsulfate reductase; iron-sulfur flavoenzyme; sulfur metabolism |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 03 May 2022 13:29 |
| Last Modified: | 03 May 2022 13:29 |
| URI: | https://pred.uni-regensburg.de/id/eprint/42489 |
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