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Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis.

Hartshorne, R. S. ; Richardson, D. J. ; Simon, J. (2006)
Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis.
In: Biochemical Society transactions, 34 (Pt 1)
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

c-Type cytochromes are a widespread class of proteins that play a vital role in the energy-conserving metabolism of prokaryotic and eukaryotic organisms. The key event in cytochrome c biogenesis is the covalent attachment of the haem cofactor to two (or rarely one) cysteine residues arranged in a haem c-binding motif such as CX(2-4)CH, CXXCK or X(3)CH. This reaction is catalysed by the membrane-bound enzyme CCHL (cytochrome c haem lyase). Different CCHLs have been described and some of them are dedicated to distinct haem c-binding motifs of cytochromes that are encoded in the vicinity of the respective CCHL gene. Various bacterial genomes contain multiple copies of CCHL-encoding genes, suggesting the presence of non-conventional or even as yet unrecognized haem c-binding motifs. This assumption is exemplified in the present study using the proteobacterium Wolinella succinogenes as a model organism whose genome encodes three CCHL isoenzymes. The discovery of a novel conserved multihaem cytochrome c (MccA) is described.

Typ des Eintrags: Artikel
Erschienen: 2006
Autor(en): Hartshorne, R. S. ; Richardson, D. J. ; Simon, J.
Art des Eintrags: Bibliographie
Titel: Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis.
Sprache: Englisch
Publikationsjahr: 2006
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Biochemical Society transactions
Jahrgang/Volume einer Zeitschrift: 34
(Heft-)Nummer: Pt 1
Kurzbeschreibung (Abstract):

c-Type cytochromes are a widespread class of proteins that play a vital role in the energy-conserving metabolism of prokaryotic and eukaryotic organisms. The key event in cytochrome c biogenesis is the covalent attachment of the haem cofactor to two (or rarely one) cysteine residues arranged in a haem c-binding motif such as CX(2-4)CH, CXXCK or X(3)CH. This reaction is catalysed by the membrane-bound enzyme CCHL (cytochrome c haem lyase). Different CCHLs have been described and some of them are dedicated to distinct haem c-binding motifs of cytochromes that are encoded in the vicinity of the respective CCHL gene. Various bacterial genomes contain multiple copies of CCHL-encoding genes, suggesting the presence of non-conventional or even as yet unrecognized haem c-binding motifs. This assumption is exemplified in the present study using the proteobacterium Wolinella succinogenes as a model organism whose genome encodes three CCHL isoenzymes. The discovery of a novel conserved multihaem cytochrome c (MccA) is described.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology
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10 Fachbereich Biologie
Hinterlegungsdatum: 07 Dez 2010 15:19
Letzte Änderung: 05 Mär 2013 09:42
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