scholarly journals Exploring the proteome associated with the mRNA encoding the D1 reaction center protein of Photosystem II in plant chloroplasts

2020 ◽  
Vol 102 (2) ◽  
pp. 369-382 ◽  
Author(s):  
Kenneth P. Watkins ◽  
Rosalind Williams‐Carrier ◽  
Prakitchai Chotewutmontri ◽  
Giulia Friso ◽  
Marlene Teubner ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Reaction Center Protein

scholarly journals Phosphorylation of the D1 Photosystem II Reaction Center Protein Is Controlled by an Endogenous Circadian Rhythm

2002 ◽  
Vol 130 (4) ◽  
pp. 2069-2075 ◽  
Author(s):  
Isabelle S. Booij-James ◽  
W. Mark Swegle ◽  
Marvin Edelman ◽  
Autar K. Mattoo
Keyword(s):  
Circadian Rhythm ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Reaction Center Protein ◽  
Endogenous Circadian Rhythm

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

1989 ◽  
Vol 86 (17) ◽  
pp. 6617-6620 ◽  
Author(s):  
B M Greenberg ◽  
V Gaba ◽  
O Canaani ◽  
S Malkin ◽  
A K Mattoo ◽  
...  
Keyword(s):  
Quantum Yield ◽  
Photosystem Ii ◽  
Protein Degradation ◽  
Reaction Center ◽  
Spectral Range ◽  
Photosynthetic Pigments ◽  
Redox States ◽  
Reaction Center Protein ◽  
Broad Spectral Range ◽  
Uv Visible

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.

Free Radical Scavengers Inhibit Light-Dependent Degradation of the 32 kDa Photosystem II Reaction Center Protein

1990 ◽  
Vol 45 (5) ◽  
pp. 412-417 ◽  
Author(s):  
Sudhir K. Sopory ◽  
Bruce M. Greenberg ◽  
Roshni A. Mehta ◽  
Marvin Edelman ◽  
Autar K. Mattoo
Keyword(s):  
Free Radical ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Electron Flow ◽  
Ultra Violet ◽  
Causative Factor ◽  
Free Radical Scavengers ◽  
Radical Scavengers ◽  
Free Radical Damage ◽  
Reaction Center Protein

Abstract Involvement of oxygen-free radicals in the rapid, light-dependent degradation of the 32 kDa photosystem II reaction center protein was investigated. The free radical scavengers propyl-gallate and uric acid inhibited 32 kDa protein degradation without affecting linear electron flow. The involvement of singlet oxygen was excluded. Protection from degradation was also afforded under ultra-violet and far-red radiations. These data implicate free-radical damage as a common step in the degradation process, and emphasize the oxygen environment as a causative factor in destabilization of the 32 kDa protein.

Sign in / Sign up

Export Citation Format

Share Document