Abstract
The accelerated decomposition of the Meisenheimer complex, 1,1-dihydro-2,4,6-trinitrocyclohexadienate, by bovine serum albumin (BSA) is reported in detail. In the pH range of 7-9 the BSA-catalyzed reaction is accelerated by a factor of about 104 relative to the rate of decomposition of the substrate alone. This catalysis requires an unprotonated base on the protein (pKa = 8.4) and can be stoichiometrically inhibited by binding of 1 equiv of pyridoxal phosphate (PP) to the protein. Chemical modification with acetic anhydride and fluorodinitrobenzene along with previous studies on the PP-BSA complex indicates that the active site of the molecule is rich in lysine and is probably coincident with a unique PP binding site in the protein. This unusual catalytic function has also been used as a sensitive probe to generate new information on some of the ligand-binding properties of the protein.
Original language | English (US) |
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Pages (from-to) | 1934-1943 |
Number of pages | 10 |
Journal | Journal of the American Chemical Society |
Volume | 97 |
Issue number | 7 |
DOIs | |
State | Published - Apr 1 1975 |
All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry