Hartshorne, R. S. ; Kern, M. ; Meyer, B. ; Clarke, T. A. ; Karas, M. ; Richardson, D. J. ; Simon, J. (2007)
A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding.
In: Molecular microbiology, 64 (4)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
In bacterial c-type cytochromes, the haem cofactor is covalently attached via two cysteine residues organized in a haem c-binding motif. Here, a novel octa-haem c protein, MccA, is described that contains only seven conventional haem c-binding motifs (CXXCH), in addition to several single cysteine residues and a conserved CH signature. Mass spectrometric analysis of purified MccA from Wolinella succinogenes suggests that two of the single cysteine residues are actually part of an unprecedented CX15CH sequence involved in haem c binding. Spectroscopic characterization of MccA identified an unusual high-potential haem c with a red-shifted absorption maximum, not unlike that of certain eukaryotic cytochromes c that exceptionally bind haem via only one thioether bridge. A haem lyase gene was found to be specifically required for the maturation of MccA in W. succinogenes. Equivalent haem lyase-encoding genes belonging to either the bacterial cytochrome c biogenesis system I or II are present in the vicinity of every known mccA gene suggesting a dedicated cytochrome c maturation pathway. The results necessitate reconsideration of computer-based prediction of putative haem c-binding motifs in bacterial proteomes.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2007 |
| Autor(en): | Hartshorne, R. S. ; Kern, M. ; Meyer, B. ; Clarke, T. A. ; Karas, M. ; Richardson, D. J. ; Simon, J. |
| Art des Eintrags: | Bibliographie |
| Titel: | A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding. |
| Sprache: | Englisch |
| Publikationsjahr: | 2007 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Molecular microbiology |
| Jahrgang/Volume einer Zeitschrift: | 64 |
| (Heft-)Nummer: | 4 |
| Kurzbeschreibung (Abstract): | In bacterial c-type cytochromes, the haem cofactor is covalently attached via two cysteine residues organized in a haem c-binding motif. Here, a novel octa-haem c protein, MccA, is described that contains only seven conventional haem c-binding motifs (CXXCH), in addition to several single cysteine residues and a conserved CH signature. Mass spectrometric analysis of purified MccA from Wolinella succinogenes suggests that two of the single cysteine residues are actually part of an unprecedented CX15CH sequence involved in haem c binding. Spectroscopic characterization of MccA identified an unusual high-potential haem c with a red-shifted absorption maximum, not unlike that of certain eukaryotic cytochromes c that exceptionally bind haem via only one thioether bridge. A haem lyase gene was found to be specifically required for the maturation of MccA in W. succinogenes. Equivalent haem lyase-encoding genes belonging to either the bacterial cytochrome c biogenesis system I or II are present in the vicinity of every known mccA gene suggesting a dedicated cytochrome c maturation pathway. The results necessitate reconsideration of computer-based prediction of putative haem c-binding motifs in bacterial proteomes. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 16 Dez 2010 08:39 |
| Letzte Änderung: | 05 Mär 2013 09:42 |
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