  It previously has been discovered that visible light irradiation of
crystalline substrates can lead to enhancement of subsequent enzymatic reaction
rates as sharply peaked oscillatory functions of irradiation time. The
particular activating irradiation times can vary with source of a given enzyme
and thus, presumably, its molecular structure. The experiments reported here
demonstrate that the potential for this anomalous enzyme reaction rate
enhancement can be transferred from one bacterial species to another coincident
with transfer of the genetic determinant for the relevant enzyme. In
particular, the effect of crystal-irradiated chloramphenicol on growth of
bacterial strains in which a transferable R-factor DNA plasmid coding for
chloramphenicol resistance was or was not present (S. panama R+, E. coli R+,
and E. coli R-) was determined. Chloramphenicol samples irradiated 10, 35 and
60 sec produced increased growth rates (diminished inhibition) for the
resistant S. panama and E. coli strains, while having no such effect on growth
rate of the sensitive E. coli strain. Consistent with past findings,
chloramphenicol samples irradiated 5, 30 and 55 sec produced decreased growth
rates (increased inhibition) for all three strains.
