The biochemistry of heme biosynthesis
Abstract
Heme is an integral part of proteins involved in multiple electron transport chains for energy recovery found in almost all forms of life. Moreover, heme is a cofactor of enzymes including catalases, peroxidases, cytochromes of the P(450) class and part of sensor molecules. Here the step-by-step biosynthesis of heme including involved enzymes, their mechanisms and detrimental health consequences caused by their failure are described. Unusual and challenging biochemistry including tRNA-dependent reactions, radical SAM enzymes and substrate derived cofactors are reported.
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Heme negatively regulates heme biosynthesis via inhibition of ALAS and stimulates heme catabolism via activating heme oxygenase 1.
“Heme itself is the most important regulator of the heme biosynthesis pathway in that it negatively regulates heme biosynthesis via the inhibition of ALAS and stimulates heme catabolism via activating heme oxygenase 1 (HO-1) [12].”
From 5-Aminolevulinic Acid as a Theranostic Agent for Tumor Fluorescence Imaging and Photodynamic Therapy (2023) · cites this paper as [12]
Cites
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Mechanisms of Cell Protection by Heme Oxygenase-1
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Self-citationCoupling Heme and Iron Metabolism <i>via</i> Ferritin H Chain
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“The hemB gene encodes the tetrapyrrole biosynthesis enzyme porphobilinogen synthase, which catalyzes an early, required step in the common pathways leading to all tetrapyrroles, including the various hemes and chlorophyll (Scheme 1) (33).”
BackgroundNitric oxide blocks cellular heme insertion into a broad range of heme proteins
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5-Aminolevulinic Acid as a Theranostic Agent for Tumor Fluorescence Imaging and Photodynamic Therapy
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- Authors
- Heinemann, I. U., Jahn, M., & Jahn, D.
- Affiliations
- Technische Universität Braunschweig (DE)
- Corresponding author
- Jahn, Martina
- Jahn, Dieter
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2008-06
- Volume
- 474
- Issue
- 2
- Pages
- 238-251
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2016750393
- Cited by
- 311
- References
- 4
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 16 · 2023: 15 · 2022: 16 · 2021: 25 · 2020: 17 · 2019: 15 · 2018: 15 · 2017: 18 · 2016: 20 · 2015: 20 · 2014: 19 · 2013: 19 · 2012: 20
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- heme biosynthesis, electron transport chain, cytochrome P450, catalase, peroxidase, cofactors, radical SAM enzymes, enzyme mechanism
- MeSH terms
- Aminolevulinic Acid, Archaea, Bacteria, Heme, Herbicides, Models, Molecular, Neoplasms, Photochemotherapy, Plants, Porphyrias, RNA, Transfer, Tetrapyrroles
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