Ferrochelatase activity and protoporphyrin IX utilization in Haemophilus influenzae

Author:

Loeb M R1

Affiliation:

1. University of Rochester Medical Center, New York 14642, USA.

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference19 articles.

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5. Deiss A. 1993. Destruction of erythrocytes p. 203-207. In G. R. Lee T. C. Bithall J. Foerster J. W. Athens and J. N. Lukens (ed.) Wintrobe's clinical hematology. Lea and Febiger Philadelphia.

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