scholarly journals A new paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II

2006 ◽  
Vol 1757 (7) ◽  
pp. 742-749 ◽  
Author(s):  
Yoshitaka Nishiyama ◽  
Suleyman I. Allakhverdiev ◽  
Norio Murata
Keyword(s):  
Reactive Oxygen Species ◽  
Photosystem Ii ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
New Paradigm

scholarly journals Reactive oxygen species leave a damage trail that reveals water channels in Photosystem II

2017 ◽  
Vol 3 (11) ◽  
pp. eaao3013 ◽  
Author(s):  
Daniel A. Weisz ◽  
Michael L. Gross ◽  
Himadri B. Pakrasi
Keyword(s):  
Reactive Oxygen Species ◽  
Photosystem Ii ◽  
Reactive Oxygen ◽  
Water Channels ◽  
Oxygen Species

scholarly journals Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

2017 ◽  
Vol 114 (11) ◽  
pp. 2988-2993 ◽  
Author(s):  
Ravindra Kale ◽  
Annette E. Hebert ◽  
Laurie K. Frankel ◽  
Larry Sallans ◽  
Terry M. Bricker ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Amino Acid ◽  
Photosystem Ii ◽  
Light Stress ◽  
Reactive Oxygen ◽  
Nonheme Iron ◽  
Oxidative Modification ◽  
Oxygen Species ◽  
Oxidatively Modified ◽  
D1 And D2 Proteins

The Photosystem II reaction center is vulnerable to photoinhibition. The D1 and D2 proteins, lying at the core of the photosystem, are susceptible to oxidative modification by reactive oxygen species that are formed by the photosystem during illumination. Using spin probes and EPR spectroscopy, we have determined that both O2•− and HO• are involved in the photoinhibitory process. Using tandem mass spectroscopy, we have identified a number of oxidatively modified D1 and D2 residues. Our analysis indicates that these oxidative modifications are associated with formation of HO• at both the Mn4O5Ca cluster and the nonheme iron. Additionally, O2•− appears to be formed by the reduction of O2 at either PheoD1 or QA. Early oxidation of D1:332H, which is coordinated with the Mn1 of the Mn4O5Ca cluster, appears to initiate a cascade of oxidative events that lead to the oxidative modification of numerous residues in the C termini of the D1 and D2 proteins on the donor side of the photosystem. Oxidation of D2:244Y, which is a bicarbonate ligand for the nonheme iron, induces the propagation of oxidative reactions in residues of the D-de loop of the D2 protein on the electron acceptor side of the photosystem. Finally, D1:130E and D2:246M are oxidatively modified by O2•− formed by the reduction of O2 either by PheoD1•− or QA•−. The identification of specific amino acid residues oxidized by reactive oxygen species provides insights into the mechanism of damage to the D1 and D2 proteins under light stress.

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