Huangen  Ding

Huangen  Ding

BMB Division

PhD: University of Pennsylvania, 1995

Phone: 225-578-4797

Lab Phone: 225-578-4731

Office: 608 Life Sciences Building
Lab: 514/601/606/607/608 Life Sciences Building
Website: Ding Lab

Area of Research Interest

Our research has focused on iron-sulfur cluster biogenesis and iron homeostasis.  While sulfur in iron-sulfur clusters in proteins is derived from L-cysteine via cysteine desulfurase, the specific iron donor has not been fully understood.  We aim to illustrate the mechanism by which the intracellular iron is mobilized and delivered for iron-sulfur cluster biogenesis in proteins.  We have also been interested in the redox regulation of iron-sulfur proteins in key physiological processes.  


Selected Publications

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.


Landry, A. P., & Ding, H. (2014) Redox Control of human mitochondrial outer membrane protein mitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide. J. Biol. Chem. 289, 4307-4315.


Tan, G., Cheng, Z., Peng, Y., Landry, A. P., Lu, J., & Ding, H. (2014) Copper binding in IscA inhibits iron-sulphur cluster assembly in Escherichia coli. Mol. Microbiol. 93,629-644.


Cheng, Z., Tan, G., Wang, W., Su, X., Landry. A. P., Lu, J., & Ding, H. (2014) Iron and zinc binding activity of Escherichia coli topoisomerase I homolog YrdD. Biometals, 27, 229-236.


Landry, A. P. & Ding, H. (2014) The N-terminal domain of human DNA helicase Rtel1 contains a redox active iron-sulfur cluster. Biomed Res Int. 2014:285791.