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Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c ‐type cytochromes
Author(s) -
Turkarslan Serdar,
Sanders Carsten,
Daldal Fevzi
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05148.x
Subject(s) - biology , escherichia coli , mutant , heme , cytochrome , biochemistry , ligation , bacteria , microbiology and biotechnology , genetics , gene , enzyme
Summary In all organisms, haem is post‐translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c ‐type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem–apocytochrome ligation per se . In this issue of Molecular Microbiology , Feissner and colleagues report that a single polypeptide from Helicobacter pylori , corresponding to the fusion of two proteins found in other organisms, performs haem ligation to a coexpressed Bordetella pertussis apocytochrome c in an Escherichia coli mutant lacking its own cytochrome c maturation proteins. This simple experimental system pinpoints the components catalysing extracytoplasmic covalent haem ligation and raises intriguing issues about the requirements for delivery of haem and apocytochrome c substrates to produce c holocytochromes.

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