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

Open access
Greenberg, B M, Gaba, V, Canaani, O, Malkin, S, Mattoo, A K, Edelman, M·1989·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Greenberg, B. M., Gaba, V, Canaani, O., Malkin, S., Mattoo, A. K., & Edelman, M.
Venue
Proceedings of the National Academy of Sciences
Published
1989-09
Volume
86
Issue
17
Pages
6617-6620
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2021978270
Cited by
304
References
0
FWCI
4.59
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions. https://app.cochat.ai/papers/10.1073/pnas.86.17.6617
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Greenberg, B. M., Gaba, V, Canaani, O., Malkin, S., Mattoo, A. K., & Edelman, M. (1989). Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.17.6617

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