The identity and reactivity of the NO. adducts of phenoxyl radicals will be probed by laser flash photolysis, stopped flow UV-vis and Fourier Transform infrared (FTIR) spectroscopy. These NO. adducts are important intermediates leading to the ultimate deactivation of a wide variety of biological systems, including Photosystem II, ribonucleotide reductase and prostaglandin H synthase. The tyrosyl free radicals known to be active in these systems have been shown to react in an unknown fashion with nitric oxide. Stopped flow spectroscopy will allow the direct measurement of reaction rates of phenoxyl radicals with NO., while FTIR spectroscopy can resolve the identity of the longer lived species produced. The project will begin with simple, stable phenoxyl radicals in non-aqueous solvents, then move to more biologically relevant phenols (tyrosine and protein models) and conditions (aqueous solutions with micelles and vesicles).

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM020393-01
Application #
6070567
Study Section
Physical Biochemistry Study Section (PB)
Program Officer
Marino, Pamela
Project Start
2000-08-01
Project End
Budget Start
2000-08-01
Budget End
2001-07-31
Support Year
1
Fiscal Year
2000
Total Cost
$32,416
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