Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli

Biochem Biophys Res Commun. 1998 Oct 29;251(3):744-7. doi: 10.1006/bbrc.1998.9549.


We report on a system to improve expression of mature c-type cytochromes in Escherichia coli. It is based on the use of plasmid pEC86 that expresses the E. coli cytochrome c maturation genes ccmABCDEFGH constitutively, whereby the production of both endogenous and foreign c-type cytochromes was increased substantially. The periplasmic soluble domains of the c-type cytochrome subunits FixO and FixP of the Bradyrhizobium japonicum cbb3 oxidase could be expressed in E. coli only when pEC86 was provided in a degP-deficient strain. This shows that a stimulation of heme attachment by the Ccm maturase system combined with the diminished proteolytic activity in the periplasm can increase c-type cytochrome yields.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bradyrhizobium / enzymology*
  • Cytochrome c Group / biosynthesis*
  • Cytochrome c Group / genetics
  • Electron Transport Complex IV / biosynthesis*
  • Electron Transport Complex IV / genetics
  • Escherichia coli / genetics
  • Membrane Proteins / biosynthesis
  • Membrane Proteins / genetics
  • Oxidoreductases / biosynthesis*
  • Oxidoreductases / genetics
  • Plasmids
  • Protein Processing, Post-Translational
  • Recombinant Proteins / biosynthesis*
  • Solubility


  • Cytochrome c Group
  • Membrane Proteins
  • Recombinant Proteins
  • cytochrome FixO
  • cytochrome FixP
  • Oxidoreductases
  • duroquinol oxidase
  • Electron Transport Complex IV