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Heme attachment to c-type cytochromes in bacteria requires cysteine thiols in the CXXCH motif of the protein. The involvement of the periplasmic disulfide generation system in this process remains unclear. We undertake a systematic evaluation of the role of DsbA and DsbD in cytochrome c biogenesis in Escherichia coli and show unequivocally that DsbA is not essential for holocytochrome production under aerobic or anaerobic conditions. We also prove that DsbD is important but not essential for maturation of c-type cytochromes. We discuss the findings in the context of a model in which heme attachment to, and oxidation of, the apocytochrome are competing processes.

Original publication

DOI

10.1016/j.febslet.2012.04.055

Type

Journal article

Journal

FEBS Lett

Publication Date

12/06/2012

Volume

586

Pages

1702 - 1707

Keywords

Bacterial Proteins, Cystine, Cytochromes c, Escherichia coli, Escherichia coli Proteins, Gene Knockout Techniques, Membrane Proteins, Oxidoreductases, Oxygen, Periplasm, Protein Disulfide-Isomerases