Far-infrared perturbation of reaction rates in myoglobin at low temperatures

We present evidence that far-infrared radiation of 50.5 ${\mathrm{cm}}^{\mathrm{-}1}$ enhances the recombination rates of photodissociated sperm whale myoglobin at temperatures below 180 K. The enhancement disappears above the glass transition of the glycerol solvent at 180 K. Control experiments show that the enhancement in recombination kinetics cannot be attributed to simple solvent heating but instead is involved with protein absorption of far-infrared radiation.