# Tracey A. Rouault
**Tracey A. Rouault** (also published as Tracey Rouault and T A Rouault) is an American physician-scientist who studies [human iron metabolism](https://www.edgepedia.org/human-iron-metabolism) and the assembly of iron-sulfur clusters, the iron-and-sulfur cofactors that many proteins need to work. She is a Senior Investigator at the Eunice Kennedy Shriver National Institute of Child Health and [Human Development](https://www.edgepedia.org/human-development) (NICHD), where she became head of the Section on Human Iron Metabolism and the Metals Biology and Molecular Medicine Branch.[1](https://irp.nih.gov/pi/tracey-rouault)
| Key facts | |
|---|---|
| Field | Human iron metabolism and mammalian iron-sulfur cluster biology[1](https://irp.nih.gov/pi/tracey-rouault) |
| Position | Senior Investigator, NICHD; became head of the Section on Human Iron Metabolism and the Metals Biology and Molecular Medicine Branch[1](https://irp.nih.gov/pi/tracey-rouault) |
| Training | Undergraduate studies at Yale (cum laude, 1973); Duke M.D. (1977); board certified in internal medicine (1982) and rheumatology (1984)[1](https://irp.nih.gov/pi/tracey-rouault) • [2](https://www.nichd.nih.gov/newsroom/news/020924-rouault) |
| NIH career | Human genetics fellow at NICHD, then head of the Section on Human Iron Metabolism, then head of the Metals Biology and Molecular Medicine Branch[1](https://irp.nih.gov/pi/tracey-rouault) |
| Signature work | Commentary "The Intestinal Heme Transporter Revealed" (Cell, 2005); cochaperone-scaffold delivery of iron-sulfur clusters to respiratory chain complexes (Cell Metabolism, 2017)[3](https://www.cell.com/cell/fulltext/S0092-8674(05)00864-0) • [4](https://www.nichd.nih.gov/newsroom/releases/040717-mitochondria) |
| Honors | American Association of Physicians; Duke Medical Center distinguished alumnus award; two NIH Director's Awards[1](https://irp.nih.gov/pi/tracey-rouault) |
## Education, training and career
Rouault graduated cum laude from Yale in 1973 and received her M.D. from Duke in 1977. At Duke she researched paroxysmal nocturnal hemoglobinuria, a life-threatening blood disease, and published her first research paper on how the immune system destroys red blood cells in patients with it.[2](https://www.nichd.nih.gov/newsroom/news/020924-rouault)
After medical school she completed both residencies at Duke and became board certified in internal medicine in 1982 and in rheumatology in 1984. She then came to NIH as a human genetics fellow in the NICHD and was promoted to head of the Section on Human Iron Metabolism, and subsequently to head of the Metals Biology and Molecular Medicine Branch.[1](https://irp.nih.gov/pi/tracey-rouault) • [2](https://www.nichd.nih.gov/newsroom/news/020924-rouault) She was elected to the American Association of Physicians, received a distinguished alumnus award from Duke Medical Center, and has twice received the NIH Director's Award for accomplishments in iron metabolism.[1](https://irp.nih.gov/pi/tracey-rouault)
## Representative work
Intestinal heme uptake. When a 2005 Cell paper reported the identification of HCP1 (heme carrier protein 1), a membrane protein with homology to bacterial metal-tetracycline transporters that mediates heme uptake in a temperature-dependent and saturable manner, Rouault wrote the accompanying commentary, "The Intestinal Heme Transporter Revealed." The commentary argued that the identification of HCP1 fills a major missing piece in understanding iron uptake and mammalian nutrition, placing heme transport alongside the duodenal iron transporters DMT1 and ferroportin (Ireg 1) identified earlier.[5](https://www.cell.com/cell/fulltext/S0092-8674(05)00644-6) • [3](https://www.cell.com/cell/fulltext/S0092-8674(05)00864-0) The discovery paper showed that HCP1 mRNA is highly expressed in the duodenum, regulated by hypoxia, and that in iron deficiency the protein localizes to the brush-border membrane of duodenal enterocytes.[5](https://www.cell.com/cell/fulltext/S0092-8674(05)00644-6)
[Iron-sulfur cluster](https://www.edgepedia.org/iron-sulfur-cluster) delivery. A study her laboratory published in Cell Metabolism in April 2017 found that a group of proteins made up of HSC20, HSPA9, and ISCU delivers iron-sulfur clusters to the Rieske iron-sulfur protein of mitochondrial Complex III, and that HSC20 also delivers clusters to Complexes I and II. Rouault noted that the findings reveal additional genes that, if confirmed, could be used to diagnose suspected mitochondrial disorders.[4](https://www.nichd.nih.gov/newsroom/releases/040717-mitochondria)
## Iron metabolism, iron-sulfur clusters and human disease
Rouault's early work involved cloning and characterizing iron regulatory proteins 1 and 2 (IRP1 and IRP2), which bind [iron-responsive elements](https://www.edgepedia.org/iron-responsive-element) in transcripts encoding ferritin, transferrin receptor 1, ferroportin, and HIF2 alpha. In iron-replete cells IRP1 acquires an iron-sulfur cluster that prevents IRE binding and lets the protein function as a cytosolic aconitase. That discovery led her laboratory into iron-sulfur cluster biogenesis, where it characterized the mammalian cysteine desulfurase NFS1, the primary scaffold ISCU, the secondary scaffold NFU1, the NFS1 binding partner ISD11, and the cochaperone HSC20.[1](https://irp.nih.gov/pi/tracey-rouault) Her review [The role of iron regulatory proteins in mammalian iron homeostasis and disease](https://doi.org/10.1038/nchembio807) appeared in Nature Chemical Biology in 2006.[6](https://doi.org/10.1038/nchembio807)
In 2009 her laboratory cloned and characterized human ISD11 and showed that it forms a stable complex in vivo with the cysteine desulfurase, which generates the inorganic sulfur needed for iron-sulfur protein biogenesis. Suppressing ISD11 in human cells inactivated both mitochondrial and cytosolic aconitases and activated IRP1's IRE-binding activity, showing that ISD11 is required for cluster assembly and for cytosolic iron homeostasis.[7](https://pmc.ncbi.nlm.nih.gov/articles/PMC2714726/) In the assembled human mitochondrial core complex, NFS1, and ISCU2 work with frataxin (FXN), the ferredoxin FDX2, and the accessory proteins ISD11 and acyl carrier protein, while the HSP70-family protein HSPA9 works with the DnaJ-type protein HSC20 to facilitate cluster transfer to recipient proteins.[8](https://www.mdpi.com/2304-6740/10/3/31) • [9](https://pmc.ncbi.nlm.nih.gov/articles/PMC8349188/)
Inherited defects in the genes that encode iron-sulfur assembly proteins cause several diseases, including Friedreich ataxia, and the list has expanded to include multiple rare diseases that often present as neuromuscular disease in children.[1](https://irp.nih.gov/pi/tracey-rouault) • [9](https://pmc.ncbi.nlm.nih.gov/articles/PMC8349188/) Her laboratory also found that mice lacking IRP2 develop adult-onset neurodegeneration with prominent motor neuron disease, and worked to identify human patients with IRP2-deficiency neurodegenerative disease. Separately, it showed that heme oxygenase 1 deficiency causes iron redistribution because the lack of HO1 kills erythrophagocytosing macrophages.[1](https://irp.nih.gov/pi/tracey-rouault)
## References
1. Tracey Ann Rouault, M.D. | NIH Intramural Research Program. https://irp.nih.gov/pi/tracey-rouault
2. Spotlight: Women in Science: Dr. Tracey Rouault on Resilience. NICHD. https://www.nichd.nih.gov/newsroom/news/020924-rouault
3. https://www.cell.com/cell/fulltext/S0092-8674(05)00864-0
4. NICHD scientists identify proteins involved in cells' energy production. NICHD, 2017. https://www.nichd.nih.gov/newsroom/releases/040717-mitochondria
5. https://www.cell.com/cell/fulltext/S0092-8674(05)00644-6
6. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nature Chemical Biology, 2006. https://doi.org/10.1038/nchembio807
7. Human ISD11 is essential for both iron–sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum Mol Genet, 2009. https://pmc.ncbi.nlm.nih.gov/articles/PMC2714726/
8. Mitochondrial De Novo Assembly of Iron–Sulfur Clusters in Mammals. Inorganics, 2022. https://www.mdpi.com/2304-6740/10/3/31
9. Outlining the Complex Pathway of Mammalian Fe-S Cluster Biogenesis. Cell Metabolism, 2021. https://pmc.ncbi.nlm.nih.gov/articles/PMC8349188/
---
*Topic: Encyclopedia › Life and health › Life and health scientists › Medical and health researchers › Hematology and blood disorder researchers › Red cell and hemoglobin researchers*
*Initially written Sep 20, 2026 · Edited: Oct 11, 2026; Oct 15, 2026*
*Copyright 2026 EdgeChat AI, a subsidiary of Biostate AI.*
License: Edgepedia Community License 1.0, https://www.edgepedia.org/edgepedia/license