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A component of the photosystem II reaction center, the 32-kDa protein, is rapidly turned over in the light. The mechanism of its light-dependent metabolism is largely unknown. We quantified the rate of 32-kDa protein degradation over a broad spectral range (UV, visible, and far red). The quantum yield for degradation was highest in the UVB (280-320 nm) region. Spectral evidence demonstrates two distinctly different photosensitizers for 32-kDa protein degradation. The data implicate the bulk photosynthetic pigments (primarily chlorophyll) in the visible and far red regions, and plastoquinone (in one or more of its redox states) in the UV region. A significant portion of 32-kDa protein degradation in sunlight is attributed to UVB irradiance.

The absorption and CD spectra of chloroplast fragments from spinach, barley and a barley mutant (chlorophyll b-minus) were studied at temperatures of 23 degrees C and --196 degrees C. The CD spectrum of wild type barley and spinach at --196 degrees C showed troughs at 640, 653, 676 and 695 nm and a maximum at 667 nm. The CD spectrum of the barley mutant at --196 degrees C consisted of a large trough at 684 nm, a small trough at 695 nm and a positive peak at 670 nm. A new feature observed at --196 degrees C but not at 23 degrees C is the trough at 640 nm. This 640 nm CD signal is missing in the CD spectrum of the barley mutant. It is attributable to the light-harvesting chlorophyll a/b protein which appears to be missing in the mutant. Another new feature, the trough at 695 nm, was observed in the CD spectra of spinach, barley and the barley mutant at --196 degrees C. The 695 nm trough appears to be sensitive to detergents and it may be due to a labile chlorophyll a.protein complex. Possible interpretations of the data are discussed.