Simon, J. ; Einsle, O. ; Kroneck, P. M. H. ; Zumft, W. G. (2004)
The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase.
In: FEBS letters, 569 (1-3)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
The -proteobacterium Wolinella succinogenes grows anaerobically by respiratory nitrite ammonification but not by denitrification. Nevertheless, it is capable of N(2)O reduction to N(2). Recently, the genome sequence of W. succinogenes revealed a nos gene cluster with intriguing features encoding a new type of N(2)O reductase. The predicted enzyme is similar to other N(2)O reductases exhibiting conservation of all residues ligating the two multinuclear copper centers but carries an unprecedented C-terminal monoheme cytochrome c domain. Notably, the N(2)O reductase pre-protein is synthesized with a Sec-dependent signal peptide, rather than the usually observed twin-arginine signal sequence, implying that the copper and heme cofactors are both incorporated in the periplasm. The nos gene cluster further consists of four adjacent open reading frames which are predicted to encode two monoheme c-type cytochromes as well as homologs of NapG and NapH. The latter proteins are thought to function in quinol oxidation coupled to cytochrome c reduction in electron transport to periplasmic nitrate reductase. While the accessory genes nosD, -F, -Y and -L are present in W. succinogenes, homologs of nosR and nosX are absent from the genome. We hypothesize that the nos gene cluster of W. succinogenes encodes a complete electron transport chain catalyzing N(2)O reduction by menaquinol, a pathway which might also be relevant to other bacteria.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2004 |
| Autor(en): | Simon, J. ; Einsle, O. ; Kroneck, P. M. H. ; Zumft, W. G. |
| Art des Eintrags: | Bibliographie |
| Titel: | The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase. |
| Sprache: | Englisch |
| Publikationsjahr: | 2004 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | FEBS letters |
| Jahrgang/Volume einer Zeitschrift: | 569 |
| (Heft-)Nummer: | 1-3 |
| Kurzbeschreibung (Abstract): | The -proteobacterium Wolinella succinogenes grows anaerobically by respiratory nitrite ammonification but not by denitrification. Nevertheless, it is capable of N(2)O reduction to N(2). Recently, the genome sequence of W. succinogenes revealed a nos gene cluster with intriguing features encoding a new type of N(2)O reductase. The predicted enzyme is similar to other N(2)O reductases exhibiting conservation of all residues ligating the two multinuclear copper centers but carries an unprecedented C-terminal monoheme cytochrome c domain. Notably, the N(2)O reductase pre-protein is synthesized with a Sec-dependent signal peptide, rather than the usually observed twin-arginine signal sequence, implying that the copper and heme cofactors are both incorporated in the periplasm. The nos gene cluster further consists of four adjacent open reading frames which are predicted to encode two monoheme c-type cytochromes as well as homologs of NapG and NapH. The latter proteins are thought to function in quinol oxidation coupled to cytochrome c reduction in electron transport to periplasmic nitrate reductase. While the accessory genes nosD, -F, -Y and -L are present in W. succinogenes, homologs of nosR and nosX are absent from the genome. We hypothesize that the nos gene cluster of W. succinogenes encodes a complete electron transport chain catalyzing N(2)O reduction by menaquinol, a pathway which might also be relevant to other bacteria. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 07 Dez 2010 15:18 |
| Letzte Änderung: | 05 Mär 2013 09:42 |
| PPN: | |
| Export: | |
| Suche nach Titel in: | TUfind oder in Google |
 |
Frage zum Eintrag |
Optionen (nur für Redakteure)
 |
Redaktionelle Details anzeigen |
Drucken
Impressum