Vorholt, J. A. and Hafenbradl, Doris and Stetter, Karl O. and Thauer, Rudolf K. (1997) Pathways of autotrophic CO2 fixation and of dissimilatory nitrate reduction to N2O in Ferroglobus placidus. ARCHIVES OF MICROBIOLOGY, 167 (1). pp. 19-23. ISSN 0302-8933, 1432-072X
Full text not available from this repository.Abstract
The strictly anaerobic Archaeon Ferroglobus placidus was grown chemolithoautotrophically on H-2 and nitrate and analyzed for enzymes and coenzymes possibly involved in autotrophic CO2 fixation. The following enzymes were found [values in parentheses = mu mol min(-1) (mg protein)(-1)]: formylmethanofuran dehydrogenase (0.2), formylmethanofuran:tetrahydromethanopterin formyltransferase (0.6), methenyltetrahydromethanopterin cyclohydrolase (10), F-420-dependent methylenetetrahydromethanopterin dehydrogenase (1.5), F-420-dependent methylenetetrahydromethanopterin reductase (0.4), and carbon monoxide dehydrogenase (0.1). The cells contained coenzyme F-420 (0.4 nmol/mg protein), tetrahydromethanopterin (0.9 nmol/mg protein), and cytochrome b (4 nmol/mg membrane protein). From the enzyme and coenzyme composition of the cells, we deduced that autotrophic CO2 fixation in F. placidus proceeds via the carbon monoxide dehydrogenase pathway as in autotrophically growing Archaeoglobus and Methanoarchaea species. Evidence is also presented that cell extracts of F. placidus catalyze the reduction of two molecules of nitrite to 1 N2O with NO as intermediate (0.1 mu mol N2O formed per min and mg protein), showing that - at least in principle - F. placidus has a denitrifying capacity.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MONOXIDE DEHYDROGENASE PATHWAY; THERMOPHILE METHANOPYRUS-KANDLERI; SP-NOV; TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE; DESULFOBACTERIUM-AUTOTROPHICUM; ARCHAEOGLOBUS-FULGIDUS; ARCHAEBACTERIA; BACTERIA; FORMYLMETHANOFURAN; METHANOGENESIS; autotrophic CO2 fixation; dissimilatory nitrate reduction; Archaeoglobus species; methanogenic; archaea; methanofuran; tetrahydromethanopterin; coenzyme F-420; cytochromes |
| 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: | 24 May 2023 08:23 |
| Last Modified: | 24 May 2023 08:23 |
| URI: | https://pred.uni-regensburg.de/id/eprint/51123 |
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