F. Bartl et al., A MODEL SYSTEM FOR THE HYDROGEN-BONDED CHAIN IN THE ACTIVE-CENTER OF THE MALTODEXTRINPHOSPHORYLASE - A FTIR STUDY, Journal of molecular structure, 377(2), 1996, pp. 193-200
Model systems for the hydrogen bonded chain in the active centre of ma
ltodextrinphosphorylase are synthesized and studied by FTIR spectrosco
py. A hydrogen bonded system between an amine, the phosphate group of
pyridoxalphosphate (PLP) and the phosphate group of glucose-1-phosphor
ic acid (GLC-1-P) causes an intense continuum in the IR spectrum, indi
cating that this hydrogen bonded chain shows large proton polarizabili
ty owing to collective proton tunnelling in multi-minima proton potent
ials. If the sodium salt of stearic acid is added to this hydrogen bon
ded chain, a very intense continuum is again observed. In addition, th
e carboxylate group of the stearic acid sodium salt becomes partially
protonated since a v(C=O) vibration of the carboxyl group arises at 16
78 cm(-1). The protons are located in this additional part of the chai
n.