Specific thiol compounds complement deficiency in c‐type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane‐bound disulphide isomerase‐like protein

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Abstract
Escherichia coli JCB606 carries a mutation in the dipZ gene, known to code for a disulphide isomerase-like protein, with the consequence that holo forms of neither exogenous nor endogenous c-type cytochromes are synthesised. This failure has been overcome by adding compounds containing thiol groups to the growth medium. Only l-Cysteine and 2-mercaptoethane sulphonic acid were effective, suggesting a (stereo)specific binding site that could be occupied by these compounds in the absence of the catalytic domain of DipZ.