Ding Lab

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Publications:

1. Bitoun, J. Wu, G. & Ding, H. (2008) Escherichia coli FtnA Acts as an Iron Buffer for Re-assembly of Iron-Sulfur Clusters in Response to Hydrogen Peroxide Stress Biometals (in press).

2. Lu, J. X., Yang, J., Tan, G. & Ding, H. (2008) Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli. Biochem J. 409, 535-543.

3. Ding, H. Yang, J., Coleman, L. & Yeung, S. (2007) Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions. J. Biol. Chem. 282, 7997-8004.

4. Yang, J., Bitoun, J. & Ding, H. (2006) Interplay of IscA and IscU in biogenesis of iron-sulfur clusters. J. Biol. Chem. 281, 27956-27963.

5. Ding, H., Harrison, K. & Lu, J. (2005) Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J. Biol. Chem. 280, 30432-30437.

6. Ding, B., Smith, E. & Ding, H. (2005) Mobilization of iron center in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. Biochem. J. 389, 797-802.

7. Ding, H., Clark, R. J. & Ding, B. (2004) IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions. J. Biol. Chem. 279, 37499-37504.

8. Ding, H. & Clark, R. J. (2004) Characterization of iron binding in IscA, an ancient iron sulfur cluster assembly protein. Biochem. J. 379, 433-440.

9. Bilder, P. W, Ding, H. & Newcomer, M. E. (2004) Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry. 43,133-139.

10. Rogers, P. A., Eide, L., Klungland, A. & Ding, H. (2003) Reversible inactivation of endonuclease III by nitric oxide via modification of its [4Fe-4S] cluster. DNA Repair. 2, 809-817.

11. Yang, W., Rogers, P. & Ding, H. (2002) Repair of nitric oxide-modified ferredoxin [2Fe-2S] clusters by cysteine desulfurase (IscS). J. Biol. Chem 277, 12868-12873.

12. Rogers, P. & Ding, H. (2001) L-cysteine-mediated destabilization of dinitrosyl iron complexes in proteins J. Biol. Chem 276, 30980-30986.

13. Demple, B, Ding, H, & Jorgensen, M. (2002) Escherichia coli SoxR protein: sensor/transducer of oxidative stress and nitric oxide. Methods Enzymol 348, 355-364.

14. Ding, H. & Demple, B. (2000) Direct Nitric Oxide Signal Transduction via Nitrosylation of Iron-Sulfur Centers in the SoxR Transcription Activator. Proc. Natl. Aca. Sci. USA ;97, 5146-5150.

15. Demple, B., Hidalgo, E. & Ding, H. (1999) Transcriptional Regulation via Redox-sensitive Iron-sulfur Centers in an Oxidative Stress Response. Biochem. Soc. Symp. 64, 115-124.

16. Ding, H. & Demple, B. (1998) Thiol-mediated Disassembly and Reassembly of [2Fe-2S] clusters in the Redox-regulated Transcription Factor SoxR Biochemistry 37, 17280-17286.

17. Ding, H. & Demple, B. (1997) In vivo Kinetics of a Redox-Regulated Transcriptional Switch. Proc. Natl. Aca. Sci. USA., 94; 8445-8449.

18. Hidalgo, E., Ding, H. & Demple, B. (1997) Redox Signal Transduction: Mutations Shifting [2Fe-2S] Clusters of the SoxR Sensor-Regulator to the Oxidized Form. Cell, 88; 121-129.

19. Bradley, T. M., Hidalgo, E., Leautaud, V., Ding, H. & Demple, B. (1997) Cysteine-to-Alanine Replacements in the E. coli SoxR Protein and the Role of the [2Fe-2S] Centers in Transcriptional Activation. Nucl. Acids. Res. 25; 1469-1475.

20. Saribas, A. S., Ding, H., Dutton, P. L. & Daldal, F. (1997) Substitutions at Position 146 of Cytochrome b affect drastically the properties of heme BL and Qo site of Rhodobacter capsulatus Cytochrome bc1 Complex. Biochim. Biophys. Acta. 1319; 99-108.

21. Hidalgo, E. Ding, H. & Demple, B. (1997) Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem. Sci. 22; 207-210.

22. Ding, H., Hidalgo, E. & Demple, B. (1996) The Redox State of [2Fe-2S] Clusters in SoxR Protein Regulates Its Activity as a Transcription Factor. J. Biol. Chem. 271; 33173-33175.

23. Ding, H. & Demple, B. (1996) Glutathione-mediated Destabilization of [2Fe-2S] Centers in the SoxR Regulatory Protein. Proc. Natl. Aca. Sci. USA., 93; 9449-9453.

24. Ding, H., Moser, C. C., Robertson, D. E., Tokito, M. K., Daldal, F. & Dutton, P. L. (1995) Ubiquinone Pair in the Qo Site Central to the Primary Energy Conversion Reactions of Cytochrome bc1 Complex. Biochemistry, 34; 15979-15996.

25. Ding, H., Daldal, F. & Dutton, P. L. (1995) Ion Pair Formation between Basic Residues at 144 of the Cyt b Polypeptide and the Ubiquinones at the Qo Site of the Cytochrome bc1 Complex. Biochemistry, 34; 15997-16003.

26. Saribas, A. S., Ding, H., Dutton, P. L. and Daldal, F. (1995) Tyrosine of Cytochrome b is Required for Efficient Electron Transfer at the Ubihydroquinone Oxidase Site (Qo site) of the Cytochrome bc1 Complex. Biochemistry, 34; 16004-16012.

27. Robertson, D. E., Ding, H., Chelminski, P.R., Slaughter, C., Hsu, J., Moomaw, C., Tokito, M., Daldal, F. & Dutton, P. L. (1993) Hydroubiquinone-cytochrome c2 Oxidoreductase from Rhodobacter capsulatus: Definition of a Minimal, Functional Isolated Preparation. Biochemistry, 32; 1310-1317.

28. Ding, H., Robertson, D. E., Daldal, F. & Dutton, P. L. (1992) Cytochrome bc1 Complex [2Fe-2S] Cluster and its Interaction with Ubiquinone and Ubihydroquinone at the Qo Site: A Double-occupancy Qo Site Model. Biochemistry, 31; 3144-3158.