| Value |
5740
1/sec
|
| Organism |
Unspecified |
| Reference |
Martin SM, Lindroth JR, Ledbetter JW. Protein dynamics of glycogen phosphorylase. Biochemistry. 1986 Oct 7 25(20):6070-6PubMed ID3098284
|
| Primary Source |
Cornish TJ, Ledbetter JW. Interactions at the active site of glycogen phosphorylase b. A new laser probe. Eur J Biochem. 1984 Aug 15 143(1):63-7PubMed ID6432537
|
| Method |
Flash excitation |
| Comments |
The enol structure of the pyridoxal-P cofactor of glycogen
phosphorylase absorbs well the 337-nm emission of the nitrogen
laser. When excited, the cofactor exhibits a transient
absorption at about 470 nm (Walters et al., 1982 Cornish &
Ledbetter, 1984a). Cornish and Ledbetter (1984a) describe
the absorption decay as the sum of two exponentials: a strong
first-order decay with a rate constant of 1.52 X E5 s^-1 and
a weak slowly decaying tail with a rate constant of 5.74 X E3
Sec^-1. The source of the strong fast decay is an excited singlet
state with the 3-OH proton of pyridoxal on the imine nitrogen
of the Schiff base linkage. See BNID 104762 |
| Entered by |
Uri M |
| ID |
104763 |