Although the structure of cross-linking molecules mainly determines the structural organization of actin filaments and with that the static elastic properties of the cytoskeleton, it is largely unknown how the biochemical characteristics of transiently cross-linking proteins (actin-binding proteins (ABPs)) affect the viscoelasticity of actin networks. In this study, we show that the macroscopic network response of reconstituted actin networks can be traced back to the microscopic interaction potential of an individual actin/ABP bond. The viscoelastic response of cross-linked actin networks is set by the cross-linker off-rate, the binding energy, and the characteristic bond length of individual actin/ABP interactions.