We are proposing to study the structure of an intermediate that is generated during the assembly of the essential tyrosyl radical/diferric cluster cofactor of the R2 subunit of ribonucleotide reductase from E coli. Stubbe and coworkers have demonstrated that this kinetically competent intermediate (called X) can generate the tyrosyl radical using rapid freeze quench (RFQ) Mvssbauer and EPR spectroscopies in conjunction with stopped flow absorption spectroscopy. Since RFQ samples can be made that consist of 60-80% X, we propose to use RFQ EXAFS to distinguish between these two structural motifs. This structural information will provide insight into the mechanism of the assembly process and broaden our understanding of oxygen activation by dinuclear iron proteins.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR001209-23S1
Application #
6658640
Study Section
Project Start
2002-03-01
Project End
2003-02-28
Budget Start
Budget End
Support Year
23
Fiscal Year
2002
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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