Mercaptopyruvate added to activated PFL generates two sulfur based radicals thereby inactivating the enzyme. For one of the radicals, hyperfine coupling to a single ~-methylene hydrogen of a disulfide radical is indicated. Deuteration of cys 418 and 419, residues required for catalysis, changes the EPR consistent with the radical being formed on a cysteine residue of the protein. Mutant enzymes C418S and C419S do not form the radical species observed.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR002583-11A1
Application #
5224150
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
11
Fiscal Year
1996
Total Cost
Indirect Cost
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