The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases

Arch Biochem Biophys. 1992 Mar;293(2):241-5. doi: 10.1016/0003-9861(92)90391-9.


Two Escherichia coli mutants that lack both cytochrome o and d terminal oxidases are able to grow with glucose as the carbon source but not with the aerobic substrates succinate or lactate. One of these, GV101, is a deletion mutant of cytochrome o and a point mutation of cytochrome d. The other, GK100, is a total deletion mutant of all the genes for both cytochromes. When these mutants were transformed with a plasmid containing the gene for the bacterial hemoglobin from Vitreoscilla, they were capable of growth in the presence of succinate or lactate and showed aerobic respiration in the presence of these substrates, unlike the parent strains. Cells transformed with a plasmid containing the gene for the hemoglobin but lacking the native promoter did not express the hemoglobin and did not respire. Membrane vesicles prepared from the cells consumed oxygen in the presence of succinate. This succinate-supported respiration decreased with successive washings of the vesicles but was restored by adding E. coli cytosol containing the hemoglobin or by adding the hemoglobin purified from Vitreoscilla. This respiration was inhibited by cyanide.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aerobiosis
  • Bacterial Proteins / genetics
  • Bacterial Proteins / pharmacology*
  • Cloning, Molecular
  • Cytochrome-c Oxidase Deficiency
  • Electron Transport
  • Electron Transport Complex IV / biosynthesis
  • Electron Transport Complex IV / genetics*
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / growth & development*
  • Genes, Bacterial
  • Hemoglobins / genetics
  • Hemoglobins / pharmacology*
  • Mutation
  • Structure-Activity Relationship
  • Thiotrichaceae / chemistry*
  • Thiotrichaceae / genetics
  • Thiotrichaceae / physiology


  • Bacterial Proteins
  • Hemoglobins
  • cytochrome o oxidase
  • Electron Transport Complex IV