Heme Metabolism and Cellular Dynamics
Summary
Heme, an iron–protoporphyrin IX complex, is synthesised through an eight-step pathway beginning and ending in the mitochondrial matrix, with several cytosolic intermediates. Ferrochelatase catalyses insertion of ferrous iron into protoporphyrin IX to yield heme, which is then incorporated into haemoproteins such as haemoglobin, cytochromes and catalases. Intracellular heme levels are tightly regulated by dedicated importers, export pumps and chaperones that shuttle labile heme to target proteins or to degradation pathways. Excess free heme promotes oxidative stress, lipid peroxidation and membrane damage, necessitating rapid scavenging by haem oxygenases that cleave the porphyrin ring to biliverdin, iron and carbon monoxide. Dynamic control of heme flux underpins critical cellular processes, including oxygen transport, mitochondrial respiration, redox signalling and transcriptional regulation. Perturbations in synthesis, trafficking or catabolism of heme contribute to disease states ranging from anaemias and porphyrias to neurodegeneration and cancer. Understanding the molecular machinery of heme handling reveals interconnections between metabolic demand, organellar homeostasis and cellular signalling networks.
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Heme Metabolism and Cellular Dynamics publication trend
The graph below shows the total number of articles in heme metabolism and cellular dynamics across all publications each year (not limited to Nature Index journals).
Technical terms
Heme: Iron–protoporphyrin IX cofactor central to oxygen transport, electron transfer and redox reactions.
Haemoprotein: Protein that contains a covalently or non-covalently bound heme group.
Labile heme pool: Transient, low-affinity heme reservoir available for signalling and protein maturation.
Ferrochelatase: Terminal mitochondrial enzyme inserting iron into protoporphyrin IX to form heme.
Haem oxygenase: Enzyme that degrades heme to biliverdin, free iron and carbon monoxide.
Trafficking: Intracellular movement of heme mediated by transporters and chaperone proteins.
Oxidative stress: Cellular damage resulting from excess reactive oxygen species often exacerbated by free heme.
References
- Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes. Frontiers in Pharmacology (2014).
- From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme. Cells (2020).
- Iron and Porphyrin Trafficking in Heme Biogenesis*. Journal of Biological Chemistry (2010).
- Glyceraldehyde-3-phosphate dehydrogenase is a chaperone that allocates labile heme in cells. Journal of Biological Chemistry (2018).
- The Multifaceted Role of Heme in Cancer. Frontiers in Oncology (2020).
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