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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1995 Jun;177(12):3613–3615. doi: 10.1128/jb.177.12.3613-3615.1995

Ferrochelatase activity and protoporphyrin IX utilization in Haemophilus influenzae.

M R Loeb 1
PMCID: PMC177073  PMID: 7768877

Abstract

Previous research showed that the heme-requiring human pathogen Haemophilus influenzae lacks the first six of the seven enzymes required for heme synthesis, starting with the precursor, 5-amino levulinic acid. In this study, I demonstrated either directly or by reasonable inference that all 57 strains of H. influenzae examined, including 2 unable to grow on protoporphyrin IX, possess ferrochelatase, which catalyzes heme formation by insertion of Fe2+ into the protoporphyrin IX nucleus and which is the last enzyme in the heme synthetic pathway. Further, I showed that this enzyme can also function in the reverse direction, releasing Fe2+ from heme.

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Selected References

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