Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd 1 ) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans
| Autor: | Roman A. Siddiqui, Kai-Uwe Vollack, Walter G. Zumft, Bärbel Friedrich, Effi Eisenmann, Peter M. H. Kroneck, U. H. Hole |
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| Rok vydání: | 1996 |
| Předmět: |
Nitrite Reductases
Nitric-oxide reductase Molecular Sequence Data ved/biology.organism_classification_rank.species Nitrous-oxide reductase Reductase Biochemistry Microbiology Thiobacillus Genetics Amino Acid Sequence Molecular Biology biology ved/biology Cytochrome P450 reductase General Medicine equipment and supplies biology.organism_classification Nitrite reductase Nitrous-oxide reductase activity Pseudomonas stutzeri Blotting Southern bacteria Oxidoreductases |
| Zdroj: | Archives of Microbiology. 165:55-61 |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/s002030050296 |
| Popis: | Cytochrome cd1-nitrite reductase and nitrous oxide reductase of Thiobacillus denitrificans were purified and characterized by biochemical and immunochemical methods. In contrast to the generally soluble nature of the denitrification enzymes, these two enzymes were isolated from the membrane fraction of T. denitrificans and remained active after solubilization with Triton X-100. The properties of the membrane-derived enzymes were similar to those of their soluble counterparts from the same organism. Nitrous oxide reductase activity was inhibited by acetylene. Nitrite reductase and nitrous oxide reductase cross-reacted with antisera raised against the soluble enzymes from Pseudomonas stutzeri. The nirS, norBC, and nosZ genes encoding the cytochrome cd1-nitrite reductase, nitric oxide reductase, and nitrous oxide reductase, respectively, from P. stutzeri hybridized with genomic DNA from T. denitrificans. Cross-reactivity and similar N-terminal amino acid and gene sequences suggest that the primary structures of the Thiobacillus enzymes are homologous to the soluble proteins from P. stutzeri. |
| Databáze: | OpenAIRE |
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