Molecular interactions in metalloproteins will be studied using resonance Raman (RR) spectroscopy as a probe of structure. Emphasis will be placed on iron-sulfur cluster, for which reliable assignments and force fields are under development. A computer modelling approach t the interpretation of Fe-S protein RR spectra is planned. The non-redox Fe-S proteins aconitase and dihydroxy acid dehydratases will be examined with a view to understanding the nature of enzyme-substrate interactions. The coupling of Fe-S cluster and siroheme chemistry in sulfite reductase will be probed. Molybdenum redox proteins will be studied to elucidate the structure of the active molybdopterin cofactor. Copper proteins will be examined in their reduced state using ultraviolet RR spectroscopy to utilize enhancement of bound ligand modes via metal->ligand charge transfer transitions.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
5R37GM013498-28
Application #
2168662
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1977-08-01
Project End
1995-03-31
Budget Start
1993-08-01
Budget End
1995-03-31
Support Year
28
Fiscal Year
1993
Total Cost
Indirect Cost
Name
Princeton University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
002484665
City
Princeton
State
NJ
Country
United States
Zip Code
08544