Department of Chemistry & Biochemistry, Montana State University
Speaker: Amanda Byer, doctoral student,
Department of Chemistry & Biochemistry,
Montana State University
Date: Thursday, October 12, 2017
Time: 3:10 PM
Place: Byker Auditorium, Chemistry & Biochemistry Building
Title: Radical SAM Enzyme Mechanism Investigations
A reception will follow the lecture.
Amanda Byer, a doctoral student in the Department of Chemistry and Biochemistry and
recipient of a Kopriva Graduate Student Fellowship, will present "Radical SAM Enzyme
Mechanism Investigations" as part of the College of Letters and Sciences's Kopriva
Science Seminar Series.
Radical SAM (S-adenosyl-L-methionine) enzymes constitute one of the largest enzyme superfamilies with ~114,000 members from all domains of life. When human radical SAM enzymes fail, disease states can ensue, including increased susceptibility to viral infection, diabetes mellitus, impaired cardiac and respiratory function, congenital heart disease, retrovirus infection and cofactor deficiencies. During catalysis, all radical SAM enzymes generate a highly reactive species, the 5’-deoxyadenosyl (dAdo) radical. However, despite its reactivity, the dAdo radical does not initiate damaging uncontrolled radical proliferation. We hypothesize that the enzyme environment constrains this radical reactivity while an iron-sulfur cluster and dAdo comprise an organometallic key intermediate. Employing various spectroscopic techniques, Byer's research investigates chemical intermediates in these radical SAM enzymes to determine how these fascinating organometallic biochemical systems function.