• Skip to main content
  • Skip to after header navigation
  • Skip to site footer
ERN: Emerging Researchers National Conference in STEM

ERN: Emerging Researchers National Conference in STEM

  • About
    • About AAAS
    • About the NSF
    • About the Conference
    • Partners/Supporters
    • Project Team
  • Conference
  • Abstracts
    • Undergraduate Abstract Locator
    • Graduate Abstract Locator
    • Abstract Submission Process
    • Presentation Schedules
    • Abstract Submission Guidelines
    • Presentation Guidelines
  • Travel Awards
  • Resources
    • Award Winners
    • Code of Conduct-AAAS Meetings
    • Code of Conduct-ERN Conference
    • Conference Agenda
    • Conference Materials
    • Conference Program Books
    • ERN Photo Galleries
    • Events | Opportunities
    • Exhibitor Info
    • HBCU-UP/CREST PI/PD Meeting
    • In the News
    • NSF Harassment Policy
    • Plenary Session Videos
    • Professional Development
    • Science Careers Handbook
    • Additional Resources
    • Archives
  • Engage
    • Webinars
    • ERN 10-Year Anniversary Videos
    • Plenary Session Videos
  • Contact Us
  • Login

Conformational Sampling of Glucose Oxidase for Bio-fuel Cell Applications

Undergraduate #137
Discipline: Chemistry and Chemical Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)

Edwin Gomez - University of New Orleans
Co-Author(s): Trang T. Tran, Nguyen Q. Tran, and Dhruva K. Chakravorty



Glucose Oxidase (GOX) is a redox enzyme that uses flavin adenine dinucleotide (FAD) as a cofactor to reduce β-D-glucose into δ-gluconolactone via a ping-pong steady-state kinetic mechanism. While it remains a candidate for developing alternative fuel cells, instability of the dimeric interface remains a concern. Electrochemistry experiments have determined that enzymatic efficiency depends upon the orientation of FAD to a carbon nanotube. Our hypothesis is that the orientation of FAD effects the conformational space sampled by the protein. Towards this we have applied computational chemistry methods to identify the way in which glycolysation reaction impacts the various oligomeric states of GOX. In close agreement with literature, molecular dynamics simulations of apo-GOX find that the protein undergoes large conformational changes that have been implicated in the modulating the glycosylation reaction. Our long-term goal is to develop computational chemistry methods in order to simulate the entire protein and electrode assembly in order to provide a means to stabilize GOX for applications in a bio-battery.

Funder Acknowledgement(s): Louisiana Board of Regents, National Science Foundation Grant - DMR – 1262904

Faculty Advisor: Dhruva Chakravorty,

Sidebar

Abstract Locators

  • Undergraduate Abstract Locator
  • Graduate Abstract Locator

This material is based upon work supported by the National Science Foundation (NSF) under Grant No. DUE-1930047. Any opinions, findings, interpretations, conclusions or recommendations expressed in this material are those of its authors and do not represent the views of the AAAS Board of Directors, the Council of AAAS, AAAS’ membership or the National Science Foundation.

AAAS

1200 New York Ave, NW
Washington,DC 20005
202-326-6400
Contact Us
About Us

  • LinkedIn
  • Facebook
  • Instagram
  • Twitter
  • YouTube

The World’s Largest General Scientific Society

Useful Links

  • Membership
  • Careers at AAAS
  • Privacy Policy
  • Terms of Use

Focus Areas

  • Science Education
  • Science Diplomacy
  • Public Engagement
  • Careers in STEM

Focus Areas

  • Shaping Science Policy
  • Advocacy for Evidence
  • R&D Budget Analysis
  • Human Rights, Ethics & Law

© 2023 American Association for the Advancement of Science