Cited by 105Porphyrin Metabolism and DisordersPorphyrin and Phthalocyanine ChemistryMetal-Catalyzed Oxygenation Mechanisms

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Terminal steps of haem biosynthesis

Dailey, H. A.·2002·Biochemical Society Transactions

DOI 10.1042/bst0300590

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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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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
DOI: 10.1042/bst0300590
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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