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PHOTODESTRUCTION OF BACTERIORHODOPSIN

Abstract— Suspensions of purple membrane fragments showed obvious signs of degradation after illumination with intense pulses of light from 10 ns frequency doubled Nd: YAG laser at 532 nm with intensity densities in excess of 1 MW/cm2. Using controlled illumination, a small fraction of the bacteriorhodopsin protein molecules were randomly destroyed in samples with a low salt concentration (12.5 mM) and pH = 7.9. Calculations using information from the changes in the optical absorbance spectrum and transient changes in the optical absorbance spectrum during the photocycle support a model where one protein molecule of the bacteriorhodopsin trimer is photodestroyed, the other two protein molecules switch to a blue state. In the blue state, the protein molecules have a red shifted absorption, with a peak near 600 nm. The blue state molecules show transient absorption changes at 656 nm that are similar to the native bacteriorhodopsin, except the O state is missing or altered. Additionally, the changes in curvature of the purple membrane fragments that occur during the photocycle of intact protein molecules are severely depressed. The addition of salts to the photodestroyed suspension can change the blue state molecules back to a state with an absorption maximum at 568 nm. The salt ions probably shield the other members of the trimer from the photodestroyed protein. In these reconstituted samples, the O state is observed at 656 nm; however, the membrane bending is not observed.