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Quinone-reactive proteins devoid of haem b form widespread membrane-bound electron transport modules in bacterial respiration.

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
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10 Fachbereich Biologie
Hinterlegungsdatum: 16 Dez 2010 08:02
Letzte Änderung: 05 Mär 2013 09:42
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