  Recently experiments showed that some biological noncovalent bonds increase
their lifetimes when they are stretched by an external force, and their
lifetimes will decrease when the force increases further. Several specific
quantitative models have been proposed to explain the intriguing transitions
from the "catch-bond" to the "slip-bond". Different from the previous efforts,
in this work we propose that the dynamic disorder of the force-dependent
dissociation rate can account for the counterintuitive behaviors of the bonds.
A Gaussian stochastic rate model is used to quantitatively describe the
transitions observed recently in the single bond P-selctin glycoprotein ligand
1(PSGL-1)$-$P-selectin force rupture experiment [Marshall, {\it et al.}, (2003)
Nature {\bf 423}, 190-193]. Our model agrees well to the experimental data. We
conclude that the catch bonds could arise from the stronger positive
correlation between the height of the intrinsic energy barrier and the distance
from the bound state to the barrier; classical pathway scenario or {\it a
priori} catch bond assumption is not essential.
