PhD: University of Pennsylvania, 1995
|Lab Phone: 225-578-4731
Office: 608 Life Sciences Building
Lab: 601/606/607/608 Life Sciences Building
Area of Research Interest
Our research has focused on the molecular mechanism by which the intracellular free iron is mobilized and delivered for iron-sulfur cluster assembly in proteins. Iron-sulfur proteins are involved in diverse physiological processes ranging from DNA replication and repair, RNA modification, protein synthesis, co-factor synthesis, energy metabolism, to signal transduction. Assembly of iron-sulfur clusters in proteins requires a coordinated delivery of iron and sulfur. Our studies have revealed that iron-sulfur cluster biogenesis not only requires the iron delivery of intracellular iron pool but also regulates intracellular iron homeostasis. The current goal of the project is to determine the interplay between iron-sulfur cluster biogenesis and intracellular iron homeostasis. We have also been interested in a mitochondrial outer membrane protein mitoNEET which binds a [2Fe-2S] cluster at its C-terminal cytosolic domain. MitoNEET has been associated with breast cancer, type II diabetes, and neurodegenerative diseases. Our studies have shown that mitoNEET has a novel electron transfer activity that may regulate glycolysis by promoting oxidation of NADH in cytosol. The current goal of this project is to determine the specific role and dynamic regulation of mitoNEET in the development of breast cancer.
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
Tasnim, H. & Ding, H. (2022) Electron transfer activity of the nanodisc-bound mitochondrial outer membrane protein mitoNEET. Free Radic. Biol. Med. 187, 50-58.
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.