Simon, J. ; Kern, M. (2008)
Quinone-reactive proteins devoid of haem b form widespread membrane-bound electron transport modules in bacterial respiration.
In: Biochemical Society transactions, 36 (Pt 5)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Many quinone-reactive enzyme complexes that are part of membrane-integral eukaryotic or prokaryotic respiratory electron transport chains contain one or more haem b molecules embedded in the membrane. In recent years, various novel proteins have emerged that are devoid of haem b but are thought to fulfil a similar function in bacterial anaerobic respiratory systems. These proteins are encoded by genes organized in various genomic arrangements and are thought to form widespread membrane-bound quinone-reactive electron transport modules that exchange electrons with redox partner proteins located at the outer side of the cytoplasmic membrane. Prototypic representatives are the multihaem c-type cytochromes NapC, NrfH and TorC (NapC/NrfH family), the putative iron-sulfur protein NapH and representatives of the NrfD/PsrC family. Members of these protein families vary in the number of their predicted transmembrane segments and, consequently, diverse quinone-binding sites are expected. Only a few of these enzymes have been isolated and characterized biochemically and high-resolution structures are limited. This mini-review briefly summarizes predicted and experimentally demonstrated properties of the proteins in question and discusses their role in electron transport and bioenergetics of anaerobic respiration.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2008 |
| Autor(en): | Simon, J. ; Kern, M. |
| Art des Eintrags: | Bibliographie |
| Titel: | Quinone-reactive proteins devoid of haem b form widespread membrane-bound electron transport modules in bacterial respiration. |
| Sprache: | Englisch |
| Publikationsjahr: | 2008 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Biochemical Society transactions |
| Jahrgang/Volume einer Zeitschrift: | 36 |
| (Heft-)Nummer: | Pt 5 |
| Kurzbeschreibung (Abstract): | Many quinone-reactive enzyme complexes that are part of membrane-integral eukaryotic or prokaryotic respiratory electron transport chains contain one or more haem b molecules embedded in the membrane. In recent years, various novel proteins have emerged that are devoid of haem b but are thought to fulfil a similar function in bacterial anaerobic respiratory systems. These proteins are encoded by genes organized in various genomic arrangements and are thought to form widespread membrane-bound quinone-reactive electron transport modules that exchange electrons with redox partner proteins located at the outer side of the cytoplasmic membrane. Prototypic representatives are the multihaem c-type cytochromes NapC, NrfH and TorC (NapC/NrfH family), the putative iron-sulfur protein NapH and representatives of the NrfD/PsrC family. Members of these protein families vary in the number of their predicted transmembrane segments and, consequently, diverse quinone-binding sites are expected. Only a few of these enzymes have been isolated and characterized biochemically and high-resolution structures are limited. This mini-review briefly summarizes predicted and experimentally demonstrated properties of the proteins in question and discusses their role in electron transport and bioenergetics of anaerobic respiration. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 16 Dez 2010 08:02 |
| Letzte Änderung: | 05 Mär 2013 09:42 |
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