Binuclear non-heme iron active sites are present in a wide variety of proteins and enzymes which perform different biological functions. This proposal will specifically investigate those sites present in sMMO, R2, D9D and frog M-ferritin to elucidate their differences in dioxygen reactivity (i.e. hydroxylation, radical generation, desaturation and ferroxidation). These differences have led to the identification of various diiron peroxy (P) and high-valent (Q and X) intermediates. While these enzymatic intermediates have been investigated, relatively little is known about their geometric and electronic structure and, more importantly, how their structure relates to reactivity. Therefore, the major objectives of this research proposal are to use biophysical spectroscopic techniques (EPR, resonance Raman and UV-vis/Near IR absorption/CDNTVH MCD) to characterize the geometric, electronic and magnetic properties of the various diiron peroxy (P) and high-valent (Q and X) intermediates in these enzymes and relevant model complexes and apply computational methodologies to gain greater insight into the mechanistic conversion between these intermediates.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM070292-01
Application #
6740052
Study Section
Special Emphasis Panel (ZRG1-F04 (20))
Program Officer
Basavappa, Ravi
Project Start
2004-02-01
Project End
2006-01-31
Budget Start
2004-02-01
Budget End
2005-01-31
Support Year
1
Fiscal Year
2004
Total Cost
$42,976
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305