Skip to main content
    Kent State University logo
    • Apply
    • Give Now
    • FlashLine Login
    • Calendars
    • Phone Directory
    • Maps & Directions
    • Search
    Menu Search
    • About
      Close
      • About Overview
      • Administration
      • Directions
      • Alumni
      • Facts & Figures
      • Faculty & Staff
      • History
      • Kent State Geauga News
      • Support the Campus
      • Twinsburg Academic Center
    • Academics
      Close
      • Academics Overview
      • Academic Advising
      • Student Accessibility Services
      • Calendars
      • Course Schedules
      • Distance & Online Learning
      • Majors & Degrees
      • Tutoring & Testing
      • Academic Learning Commons
      • Academic Workshops
      • Drop-Ins
      • Final Exam Schedule
      • New Student FAQs
      • Student Services Staff
    • Admissions
      Close
      • Admissions Overview
      • Apply Now
      • Referred to Regional Campus
      • Visit Campus
      • Newly Admitted Students
      • Placement Testing
      • College Credit Plus
      • Tuition & Fees
      • Financial Aid
      • Scholarships
      • Experienced Learner 60+ Program (Formerly "Senior Guest")
      • Meet the Flashes
      • Request Information
      • Transfer Students
      • Ohio College Comeback
    • Campus Life
      Close
      • Campus Life Overview
      • Flash Bistro
      • Annual Scholarship Award Reception
      • Bookstore
      • Career Services
      • Clubs & Organizations
      • Community Job Openings
      • Computer Labs
      • Counseling Services
      • Rising Scholars Program
      • Technology Help
      • Wellness Initiative
      • Commencement
    • Community & Partnerships
      Close
      • Community & Partnerships Overview
      • Events & Room Reservations
      • Outreach & Partnerships
      • Programs & Presentations
      • Student Discounts
      • Workforce Development - Geauga
      • Workforce Development - Twinsburg
    • Locations
      Close
      • Locations Overview
      • Ashtabula
      • East Liverpool
      • Kent
      • Salem
      • Stark
      • Trumbull
      • Tuscarawas
      • Regional Campuses
      • Other U.S. Academic Locations
      • Kent State Worldwide
    • Campus Safety
      Close
      • Campus Safety Overview
      • A.L.I.C.E. Training Workshops
      • CARE Team
      • Campus Safety Staff
      • Annual Security Reports
      • Smoke-Free, Tobacco-Free University
    • FlashLine Login
    • Calendars
    • Phone Directory
    • Maps & Directions
    • Search
    • Apply
    • Give Now
    Live Chat
    Zhiqiang Molly Wang

    Zhiqiang Wang, Ph.D.

    Professor
    Campus:
    Geauga
    Contact Information
    Email:
    zwang3@kent.edu
    Phone:
    330-339-3391

    Biography

    Our research interests in a broad sense are to understand the biological functions of certain proteins from their structural point of views. Particularly, we focus on structure-function relationships of metalloenzymes, as well as protein-protein interaction and protein-ligand interactions that are related to signal transductions in cells. Our long-term goal is to translate these basic research studies into the discovery of new drugs and therapeutic methods to treat human diseases.

    Our research interests are in the following areas:

    1. Regulation of Nitric Oxide Synthesis in Bacterial Nitric Oxide Synthase (NOS)
    2. Receptor and Protein Interactions in NO Signaling
    3. Structure-function Studies of Heme O2 and NO Sensors
    4. Mechanism of NOS-related Endothelial Dysfunction

    Scholarly, Creative & Professional Activities

    1. Tejero, J., Biswas, A., Haque, M.M., Wang, Z.-Q., Hemann, C., Varnado, C.L., Novince, Z., Hille, R., Goodwin. D.C., Stuehr, D.J. “Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase.” Biochem. J. 433, 163-74, 2010.
    2. Wang, Z.-Q., Wei, C.-C., and Stuehr, D. J. “How Does A Valine Residue That Modulates Heme-NO Binding Kinetics in Inducible NO Synthase Regulate Enzyme Catalysis” J Inorg. Biochem. 104, 349-56, 2009. 
    3. Wei, C.-C., Wang, Z.-Q., Tejero J, Yang YP, Hemann C, Hille R and Stuehr D. J. “Catalytic reduction of a tetrahydrobiopterin radical within nitric-oxide synthase.” J. Biol. Chem., 283, 11734-42, 2008. 
    4. Wang, Z.-Q., Lawson R. J., Madhavan, B. R., Wei, C.-C., Crane, B. R., Munro, A.W., and Stuehr, D. J. “Bacterial Flavodoxin Support Nitric Oxide Production by Bacillus Subtilis Nitric-Oxide Synthase.” J. Biol. Chem., 282, 2196-202, 2007. 
    5. Wang, Z.-Q., Wei, C.-C., Santolini, J., Koustubh, P., Wang, Q. and Stuehr, D. J. “A Tryptophan That Modulates Tetrahydrobiopterin-Dependent Electron Transfer in Nitric Oxide Synthase Regulates Enzyme Catalysis by Additional Mechanisms.” Biochemistry, 44, 4676-90, 2005.
    6. Wang, Z.-Q., Wei, C.-C., Sharma, M., Pant, K., Crane, B. R., and Stuehr, D. J. “A Conserved Val to Ile Switch Near the Heme Pocket of Animal and Bacterial Nitric-Oxide Synthases Helps Determine Their Distinct Catalytic Profiles. J. Biol. Chem., 279, 19018-25, 2004.
    7. Wang, Z.-Q., and Stuehr D. J. “Calcium Signaling: NO Synthase”, Encyclopedia of Biological Chemistry, Edited by William J Lennarz, Deniel M lane, Academic Press, 256-260, Sep 2004.
    8. Wei, C.-C., Wang, Z.-Q., Arvai A. S., Hemann, C., Hille, R., Getzoff E. D., and Stuehr, D. J. “Structure of Tetrahydrobiopterin Tunes Its Electron Transfer to the Heme-dioxy Intermediate in Nitric oxide synthase.” Biochemistry, 42, 1969-77, 2003. 
    9. Cao, C.-Y., Zhang, Q., Wang, Z.-Q., Wang, Y.-H., Wu, H.-M., and Huang, Z.-X. “1H-NMR Studies of the Effect in Heme of Cytochrome b5 Caused by Valine45 Site-directed Mutation.” Biochemie, 85, 1007-1016, 2003.
    10. Wang, Z.-Q., Wei, C.-C., and Stuehr, D.J. "A Conserved Tryptophan 457 Modulates the Kinetics and Extent of N-hydroxy-L-Arginine Oxidation by Inducible Nitric Oxide Synthase” J. Biol. Chem., 277, 12830, 2002.
    11. Wang, Z.-Q., Wei, C.-C., Ghosh S, Meade, A. L., Hemann, C., Hille, R., and Stuehr D. J. "A Conserved Trytophan In Nitric Oxide Synthesis Regulates Heme-dioxy Reduction by Tetrahydrobiopterin" Biochemistry, 40(43), 12819-25, 2001.
    12. Wang, Z.-Q., Wang Y.-H., Wang W.-H., Xue, L.-L., Wu, X.-Z., Xie, Y., and Huang Z.-X., "The Effect of Mutation at Valine-45 on the Stability and Redox Potentials of Trypsin-cleaved Cytochrome b5", Biophysical Chemistry, 83(1), 3-17, 2000.
    13. Wang, Z.-Q., Wang Y.-H., Qian, W., Wang H.-H., Chunyu, L.-J., Xie, Y., and Huang Z.-X., "Methanol-induced Unfolding and Refolding of Cytochrome b5 and Its P40V Mutant Monitored by UV-visible, CD and Fluorescence Spectra", J. Protein Chem., 18(5), 547-55, 1999.
    14. Zhu B., Wang Z.-Q., Li, X.-M., Zhao D.-Q., and Ni, J.-Z., “Lanthanide Metal Complexes for the Hydrolysis of Ribonucleoside 3’,5’-cyclic Phosphate and Deoxyribonucleoside 3’, 5’-cyclic Phosphate”, Journal of Molecular Catalysis A-Chemical, 118(1). L5-L7, 1997. 
    15. Wang, Z.-Q., Zhang S.-G. Liu, Q.-M., and Ni, J.-Z., "Studies on The Action of Rare Earth with Bovine Serum Albumin in Multimolecular System", Journal of Rare Earth (Special Issue), 573, 1995.

    Geauga Campus Mailing Address

    14111 Claridon-Troy Road
    Burton, OH 44021

    Geauga Campus Street Address

    14111 Claridon-Troy Road
    Burton, OH 44021

    Twinsburg Academic Center Mailing Address

    2745 Creekside Drive
    Twinsburg, OH 44087

    Twinsburg Academic Center Street Address

    2745 Creekside Drive
    Twinsburg, OH 44087

    Contact Us
    GeaugaAdmissions@kent.edu

    • Geauga Campus Phone
      440-834-4187

    • Twinsburg Academic Center Phone
      330-888-6400

    • facebook
    • linkedin
    • X
    • instagram
    • ...
    Information
    • Annual Security Report -Geauga
    • Annual Security Report -Twinsburg Academic Center
    • Campus Safety
    • For Our Alumni
    • Hours of Operation
    • Jobs & Employment
    • Privacy Statement
    • Website Feedback Form
    Kent State University logo
    © 2025 Kent State University All rights reserved.