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. 1989 Sep;86(17):6617–6620. doi: 10.1073/pnas.86.17.6617

Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions.

B M Greenberg 1, V Gaba 1, O Canaani 1, S Malkin 1, A K Mattoo 1, M Edelman 1
PMCID: PMC297895  PMID: 2671998

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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