Hydrolysis and reduction of factor 390 by cell extracts of Methanobacterium thermoautotrophicum (strain delta H)
| Autor: | Godfried D. Vogels, Jan T. Keltjens, Servé W. M. Kengen, C. van der Drift, H. W. Von Den Hoff |
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| Rok vydání: | 1991 |
| Předmět: |
Hydrogenase
Stereochemistry Riboflavin Methanobacteriaceae Euryarchaeota Microbiology Cofactor Hydrolysis chemistry.chemical_compound Flavins Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification biology Spectrum Analysis Substrate (chemistry) biology.organism_classification Adenosine Monophosphate Coenzyme F420 Enzyme Biochemistry chemistry Ionic strength biology.protein Oxidation-Reduction Research Article |
| Zdroj: | Journal of Bacteriology. 173:2283-2288 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.173.7.2283-2288.1991 |
| Popis: | Cell extracts of Methanobacterium thermoautotrophicum (strain delta H) were found to perform a hydrogen-dependent reduction of factor 390 (F390), the 8-adenylyl derivative of coenzyme F420. Upon resolution of cell extracts, F390-reducing activity copurified with the coenzyme F420-dependent hydrogenase. This indicates that F390 serves as a substrate of that enzyme. Activity towards F390 was approximately 40-fold lower than that towards coenzyme F420 (0.12 and 5.2 mumol.min-1.mg of protein-1, respectively). In addition, cell extracts catalyzed the hydrolysis of F390 to AMP and coenzyme F420. This hydrolysis required the presence of thiols (6 mM) and much ionic strength (1 M KCl) and was reversibly inhibited by oxygen. The reaction proceeded optimally at pH 8.2 and was Mn dependent. Conditions for F390 hydrolysis in cell extracts are in many respects opposite to those previously described for F390 synthesis. |
| Databáze: | OpenAIRE |
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