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Ferrochelatase activity and protoporphyrin IX utilization in Haemophilus influenzae
1University of Rochester Medical Center, New York 14642, USA.
Journal of Bacteriology
|June 1, 1995
Summary
The human pathogen Haemophilus influenzae possesses ferrochelatase, the final enzyme in heme synthesis. This enzyme can also function in reverse, releasing iron from heme.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Haemophilus influenzae is a heme-requiring human pathogen.
- H. influenzae lacks the initial six enzymes of the heme synthesis pathway, starting from 5-amino levulinic acid.
Purpose of the Study:
- To investigate the presence and function of ferrochelatase in H. influenzae.
- To determine if ferrochelatase activity is conserved across different strains of H. influenzae.
Main Methods:
- Enzyme assays were performed on 57 strains of H. influenzae.
- Direct and inferred evidence were used to confirm enzyme presence and activity.
Main Results:
- All 57 examined strains of H. influenzae possess ferrochelatase.
- Ferrochelatase catalyzes the final step of heme synthesis by inserting Fe2+ into protoporphyrin IX.
- The enzyme demonstrated a reverse function, releasing Fe2+ from heme.
Conclusions:
- Ferrochelatase is present in all tested H. influenzae strains, despite the absence of earlier heme synthesis enzymes.
- This enzyme plays a crucial role in heme metabolism for H. influenzae.
- The dual function of ferrochelatase (heme synthesis and degradation) may be significant for the pathogen's survival.