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Terminal steps of haem biosynthesis
Abstract
The terminal three steps in haem biosynthesis are the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX, followed by the six-electron oxidation of protoporphyrinogen to protoporphyrin IX, and finally the insertion of ferrous iron to form haem. Interestingly, Nature has evolved distinct enzymic machinery to deal with the antepenultimate (co-proporphyrinogen oxidase) and penultimate (protoporphyrinogen oxidase) steps for aerobic compared with anaerobic organisms. The terminal step is catalysed by the enzyme ferrochelatase. This enzyme is clearly conserved with regard to a small set of essential catalytic residues, but varies significantly with regard to size, subunit composition, cellular location and the presence or absence of a [2Fe-2S] cluster. Coproporphyrinogen oxidase and protoporphyrinogen oxidase are reviewed with regard to their enzymic and physical characteristics. Ferrochelatase, which is the best characterized of these three enzymes, will be described with particular emphasis paid to what has been learned from the crystal structure of the Bacillus subtilis and human enzymes.
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“There are two forms of CPO: oxygen-dependent found in aerobic organisms, and oxygen-independent, in anaerobic and facultative bacteria [21].”
From Aminolevulinic Acid (ALA) as a Prodrug in Photodynamic Therapy of Cancer (2011) · cites this paper as [21]
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Synthetic Analogues Relevant to the Structure and Function of Zinc Enzymes
Parkin, G. (2004) · Chemical Reviews · doi:10.1021/cr0206263 · Cited by 935
Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins
Rajagopal, A., Rao, A. U., Amigo, J., Tian, M., Upadhyay, S. K., Hall, C., Uhm, S., Mathew, M. K., Fleming, M. D., Paw, B. H., et al. (2008) · Nature · doi:10.1038/nature06934 · Cited by 316
The biochemistry of heme biosynthesis
Heinemann, I. U., Jahn, M., & Jahn, D. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.02.015 · Cited by 311
Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes
Layer, G., Moser, J., Heinz, D. W., Jahn, D., & Schubert, W. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg598 · Cited by 296
Aminolevulinic Acid (ALA) as a Prodrug in Photodynamic Therapy of Cancer
Wachowska, M., Muchowicz, A., Firczuk, M., Gabrysiak, M., Winiarska, M., Wańczyk, M., Bojarczuk, K., & Golab, J. (2011) · Molecules · doi:10.3390/molecules16054140 · Cited by 265
Metadata
- Authors
- Dailey, H. A.
- Affiliations
- University of Georgia (US)
- Corresponding author
- Dailey, H. A.
- ORCID
- Dailey, H. A.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2002-08-01
- Volume
- 30
- Issue
- 4
- Pages
- 590-595
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W1985614068
- Cited by
- 105
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2022: 4 · 2021: 1 · 2020: 1 · 2019: 3 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 7
- FWCI
- 2.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R56DK032303, R01DK032303)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Physical Sciences › Materials Science › Materials Chemistry › Porphyrin and Phthalocyanine Chemistry
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- heme biosynthesis, protoporphyrinogen oxidase, coproporphyrinogen oxidase, ferrochelatase, protoporphyrinogen IX, coproporphyrinogen III, oxidative decarboxylation, [2Fe-2S] cluster, crystal structure
- MeSH terms
- Bacillus subtilis, Coproporphyrinogen Oxidase, Ferrochelatase, Heme, Crystallography, X-Ray
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