• 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

The HmuT Protein in the Heme Uptake Pathway of Corynebacterium diphtheriae

Undergraduate #138
Discipline: Chemistry and Chemical Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)

Cyrianne Keutcha - Georgia State University
Co-Author(s): Elizabeth Bennett and Dabney Dixon, Georgia State University, Atlanta, GA Michael Schmitt, Food and Drug Administration, Silver Spring, MD



Strategies to use heme as a source of iron are key to the survival and virulence of many bacteria; inhibition of iron uptake pathways may be a new strategy to prevent bacterial infection. Corynebacterium diphtheriae is a Gram-positive, pathogenic bacterium that is the causative agent of diphtheria. It utilizes heme uptake pathways to obtain required heme iron. One uptake pathway involves an ABC-type transporter encoded by the hmuTUV genes. We analyze the role of HmuT, the protein that donates heme to the ABC transporter. We hypothesize that the protein residues in the binding pocket control heme release in HmuT. Mutants studied include H136A, Y235A, Y272A, and M292A. We have used chemical and thermal denaturation to observe the effects of mutation of these key amino acids on the unfolding of the protein. We have shown that H136 and Y235 are axial ligands to the heme; M292 appears to buttress the axial tyrosine. Y272, in the heme pocket as well, also affects heme binding. Future work will involve study of the proteins as a function of pH.

Funder Acknowledgement(s): Research Corporation

Faculty Advisor: Dabney Dixon,

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