Huangen Ding
Professor
BMB Division
PhD: University of Pennsylvania, 1995
Phone: 225-578-4797
Lab Phone: 225-578-4731
Office: 608 Life Sciences Building
Lab: 601/606/607/608 Life Sciences Building
E-mail: hding@lsu.edu
Area of Research Interest
Iron-sulfur proteins are involved in diverse physiological processes ranging from DNA replication and repair to RNA modification, biosynthesis of protein and co-enzymes, energy metabolism, and signal transduction. However, the mechanism by which iron-sulfur clusters are assembled in protein has not been fully understood. Our research has focused on the mechanism by which intracellular free iron is mobilized for iron-sulfur cluster assembly and on the regulation of iron homeostasis via the transcription factor ferric uptake regulator (Fur) in bacteria. We are also interested in understanding the specific functions of iron-sulfur clusters in the mitochondrial outer membrane protein mitoNEET in human cells. MitoNEET binds a redox active [2Fe-2S] cluster at its C-terminal cytosolic domain and has been linked to human diseases including breast cancer, type II diabetes, and neurodegenerative diseases. We have demonstrated that mitoNEET is a novel redox enzyme that catalyzes NADH oxidation in cytosol and promotes glycolysis in human cells. Currently, we are searching for small molecules that interact with mitoNEET to modulate energy metabolism of mitochondria in human cells
Selected Publications
Purcell, A., G., Fontenot, C. R., and Ding, H. (2024) Iron-sulfur cluster assembly scaffold protein IscU is required for activation of ferric uptake regulator (Fur) in Escherichia coli. PMID: 38452854. DOI: 10.1016/j.jbc.2024.107142.
Fontenot, C. R. & Ding, H. (2023) The C-terminal domain of the ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to sense the intracellular free iron content in Escherichia coli. Biometals PMID: 37344741 DOI: 10.1007/s10534-023-00517-6.
Fontenot, C. R. & Ding, H. (2023) Fontenot, C. R. & Ding, H. (2023) Ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to regulate intracellular iron homeostasis in Escherichia coli. J. Biological Chem. 299, 104748. PMID: 37100285 PMC10318462 DOI: 10.1016/j.jbc.2023.104748.
Tasnim, H. & Ding, H. (2022) Electron transfer activity of the nanodisc-bound mitochondrial outer membrane protein mitoNEET. Free Radic. Biol. Med. 187, 50-58. PMID: 35609862 DOI: 10.1016/j.freeradbiomed.2022.05.011.
Fontenot, C. R., Cheng, Z., & Ding, H. (2022) Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and inhibits electron transfer activity. Frontiers in Molecular Biosciences. https://doi.org/10.3389/fmolb.2022.995421.
Fontenot, C. R. & Ding, H. (2022) Ferric uptake regulators (Fur) from Vibrio cholerae and Helicobacter pylori bind a [2Fe–2S] cluster in response to elevation of intracellular free iron content. Biometals, 35, 591-600.
Fontenot, C. R., Tasnim, H., Valdes, K. A., Popescu, C. V. & Ding, H. (2020) Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli. J. Biol. Chem. 295, 15454-15463.
Tasnim, H., Landry, A. P., Fontenot, C. R., & Ding, H. (2020) Exploring the FMN binding site in the mitochondrial outer membrane protein mitoNEET. Free Radic. Biol. Med. 156, 11-19.
Wang, Y., Lee, Y., & Ding, H., (2019) Light-induced release of nitric oxide from the nitric oxide-bound CDGSH-type [2Fe-2S] clusters in mitochondrial protein Miner2. Nitric Oxide 89, 96-103.
Li, X., Wang, Y., Tan, G., Lyu, J. & Ding, H. (2018) Electron transfer kinetics of the mitochondrial outer membrane protein mitoNEET. Free Radic. Biol. Med. 121, 98-104.
Tan G, Yang J, Li T, Zhao J, Sun S, Li X, Lin C, Li J, Zhou H, Lyu J, & Ding H. (2017) Anaerobic copper toxicity and iron-sulfur cluster biogenesis in Escherichia coli. Appl Environ Microbiol. 83(16). e00867-17.
Wang, Y., Landry, A. P. & Ding, H. (2017) The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone. J. Biol. Chem. 292:10061-1006.
Cheng, Z., Landry, A. P., Wang, Y. & Ding, H. (2017) Binding of nitric oxide in the CDGSH-type [2Fe-2S] clusters of human mitochondrial protein Miner2. J. Biol. Chem.292, 3146-3153.
Landry, A. P., Wang, Y., Cheng, Z., Crochet, R.B., Lee, Y.H., & Ding, H. (2017) Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET. Free Radic. Biol. Med. 102, 240-247.
Ding, H. (2016) Iron Homeostasis and Iron-Sulfur Cluster Assembly in Escherichia coli in book Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria Publisher, Wiley-Blackwell. pp. 203-214.
Yang, J., Tan, G., Zhang, T., White, R. H., Lu, J., & Ding H. (2015) Deletion of the proposed iron chaperones IscA/SufA results in accumulation of a red intermediate cysteine desulfurase IscS in Escherichia coli. J. Biol. Chem. 290, 14226-14234.
Landry, A. P., Cheng, Z., & Ding, H. (2015) Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase. Free Radic. Biol. Med. 81, 119-127.
Huang, C. Y, Abe, Y., Ding, H. & Chung, I.F. (2015) Helicase and its interacting factors: regulation mechanism, characterization, structure, and application for drug design. Biomed. Res. Int. 2015, 909047.