Magnetic Field Effects on the Behavior of Radicals in Protein and DNA Environments

We have examined the behavior of radical pairs derived by hydrogen abstraction of triplet benzophenone and some of its derivatives from bovine serum albumin, human serum albumin and calf thymus DNA. They have been investigated by means of nanosecond laser flash photolysis techniques. The dynamics of radical pair behavior are shown to be sensitive to external magnetic fields; these effects are interpreted using the established model for the influence of magnetic fields on radical pairs in micellar aggregates, in which intersystem crossing of the radical pair is slowed by the external magnetic field. Our results indicate that proteins and DNA can confine the radicals for a sufficiently long period of time for spin evolution to be affected by external fields. In proteins the radical pair retains its geminate character (i.e. remains confined) for about 0.5-1 microsecond. Interestingly, the magnetic field effects observed in proteins and in DNA seem to occur in distinct timescales; for example, for 2,3,4,5,6-pentafluorobenzophenone bound to DNA, the magnetic field alters the radical reactivity only over times < or = 50 ns, suggesting poor confinement. The timescale for these effects can be increased by promoting Coulombic attraction between DNA and the radical precursor. Electron transfer interactions play a role in the case of DNA.