ReviewProtein science : a publication of the Protein Society2010
Structure and function of enzymes in heme biosynthesis.
Review in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
141 citing papers in PubMed, 356 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Phototrophicity and genomic composition in plant-associated Sphingomonas faeni strains.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026Article
- Genome-wide CRISPR screen reveals CGS-15943 induced heme-dependent cell death mediated by aryl hydrocarbon receptor in lung cancer cells.Apoptosis : an international journal on programmed cell death · 2026Article
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Transcriptomic dissection of floral identity and trichome-derived metabolite pathways in Cannabis sativa L.Planta · 2026Article
- Environmental Concentrations of Herbicide Prometryn Increase the Susceptibility of Reef-Building Corals to Nitrate Stress.Environmental science & technology · 2026Article
- Introduction of regioselective bacterial heme oxygenases into Arabidopsis hy1-1 supports the retrograde heme signaling hypothesis.Plant physiology · 2026Article
- Salmonella-derived haem inhibits macrophage phagocytosis and promotes infection in mice.Nature microbiology · 2026Article
- Radiometric and spectral characterization of multipanel planar light-emitting devices: a generalizable irradiance mapping approach for dose estimation.Journal of biomedical optics · 2026Article
- Article
- Infrared Photobiomodulation Modulates PpIX Production After Topical Methyl Aminolevulinate in Normal Human Skin: An Exploratory Study.Journal of biophotonics · 2026Article
- Core-Periphery Microbiota Organization Is Associated with Functional Resilience in High Arctic Svalbard Soils.Computational and structural biotechnology journal · 2026Article
- CPOP1 is a key enzyme required for nodule microenvironment control and successful symbiotic nitrogen fixation in Lotus japonicus.Journal of integrative plant biology · 2025Article
- Pathogenesis and clinical management of liver damage in porphyrias: Mechanisms and therapeutic approaches.World journal of hepatology · 2025Review
- Engineering the cytochrome P450 to enhance parthenolide production inSynthetic and systems biotechnology · 2025Article
- Evolutionary-conserved RLF, a cytochrome bThe New phytologist · 2025Article
- β‑Selective Addition of Pyrroles to Electron-Deficient Alkenes in Both Catalytic and Stoichiometric Modes on B(CACS omega · 2025Article
- Gut microbiome and blood biomarkers reveal differential responses to aerobic and anaerobic exercise in collegiate men of diverse training backgrounds.Scientific reports · 2025Article
- Article
- A Narrowband 635 nm Autofluorescence Peak in Albino Mouse Eyes Found With Multi-Modal Imaging Reveals the Presence of Protoporphyrin IX in the Choroid.Investigative ophthalmology & visual science · 2025Article
81 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetrapyrroles like hemes, chlorophylls, and cobalamin are complex macrocycles which play essential roles in almost all living organisms. Heme serves as prosthetic group of many proteins involved in fundamental biological processes like respiration, photosynthesis, and the metabolism and transport of oxygen. Further, enzymes such as catalases, peroxidases, or cytochromes P450 rely on heme as essential cofactors. Heme is synthesized in most organisms via a highly conserved biosynthetic route. In humans, defects in heme biosynthesis lead to severe metabolic disorders called porphyrias. The elucidation of the 3D structures for all heme biosynthetic enzymes over the last decade provided new insights into their function and elucidated the structural basis of many known diseases. In terms of structure and function several rather unique proteins were revealed such as the V-shaped glutamyl-tRNA reductase, the dipyrromethane cofactor containing porphobilinogen deaminase, or the "Radical SAM enzyme" coproporphyrinogen III dehydrogenase. This review summarizes the current understanding of the structure-function relationship for all heme biosynthetic enzymes and their potential interactions in the cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.