AbstractAt least four different excited states were observed in various proteins under uv excitation; one with a band peaking at wavelengths around 410 nm and one band which peaks at around 370 nm. The former is ascribed to CO bonds since a very similar band appears in many highly purified materials not containing aromatic rings but only CO or peptide bonds; such as polyglutamic acid, cyclohexanone, acetamide and some sugars, for instance. This band is observed in many proteins and can also be excited with 365 nm. The 370 nm band appears preferentially in proteins of globular structure and is excited only in a relatively narrow excitation band around 310 nm.The blue is always accompanied, in proteins as well as in the above‐mentioned non‐aromatic compounds, by a short‐living (∼0.5 sec decay time at 77°K) phosphorescence, with slightly larger wavelength than the fluorescence. There is further a long‐living phosphorescence band (decay time several seconds at 77°K) also in the blue. Its decay time is strongly dependent upon the environment. It is observed in many globular proteins and in non‐protein CO containing materials, but not in fibrous proteins such as collagen, as yet. Its decay time is particularly long in globular proteins such as in eggwhites. In cyclohexanone‐Me‐pentan solutions the lifetime of this band is long, in EPA glass it is much shorter. The species from which the longtime phosphorescence originates could be picked up as EPR signals by the half field strength method.For all materials investigated (proteins, tyrosin, cyclohexanone) the g‐values are the same, but they depend on the environment, indicating a strong interaction with the surroundings. In Me‐pentan solutions the g‐value is smaller than in the solid material. Prolonged irradiation reduces the concentration of these excited species. Because of the various decay times and their dependence on the environment, many proteins do not exhibit a decay composed of one or two exponentials, but display a more complicated decay.
Read full abstract