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Updated: Jul 17, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Terminal steps of haem biosynthesis
1Biomedical and Health Sciences Institute, A222 Life Science Building, University of Georgia, Athens, GA 30602-7229, USA. hdailey@uga.edu
Nature uses different enzymes for heme biosynthesis in aerobic versus anaerobic organisms. The final enzyme, ferrochelatase, is conserved but varies across species, with insights from crystal structures.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Heme biosynthesis involves three terminal steps: oxidative decarboxylation, oxidation, and iron insertion.
- Enzymatic machinery for heme synthesis differs between aerobic and anaerobic organisms for key steps.
- Ferrochelatase catalyzes the final step of inserting ferrous iron to form heme.
Purpose of the Study:
- To review the enzymic and physical characteristics of coproporphyrinogen oxidase and protoporphyrinogen oxidase.
- To describe ferrochelatase, focusing on structural insights from Bacillus subtilis and human enzymes.
- To highlight conserved and variable features of ferrochelatase across different organisms.
Main Methods:
- Review of existing literature on heme biosynthesis enzymes.
- Analysis of enzymic and physical characteristics of oxidases.
- Examination of crystal structures of Bacillus subtilis and human ferrochelatase.
Main Results:
- Distinct enzymes (coproporphyrinogen oxidase, protoporphyrinogen oxidase) are employed in aerobic vs. anaerobic heme synthesis.
- Ferrochelatase shows conserved catalytic residues but significant variation in size, subunit composition, and cellular location.
- The [2Fe-2S] cluster is present in some ferrochelatase enzymes, but absent in others.
- Crystal structures reveal detailed information about the Bacillus subtilis and human ferrochelatase enzymes.
Conclusions:
- Organisms have evolved specialized enzymes for heme biosynthesis, adapting to aerobic or anaerobic conditions.
- Ferrochelatase is a crucial, conserved enzyme in heme production, with structural diversity.
- Structural studies of ferrochelatase provide valuable insights into its mechanism and evolutionary conservation.
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