6533b7d5fe1ef96bd1263e3f

RESEARCH PRODUCT

Studies on the mechanism of photosystem II photoinhibition II. The involvement of toxic oxygen species.

Wolfgang RühleAloysius WildMichael Richter

subject

PhotoinhibitionbiologyPhotosystem IIChemistryRadicalCell BiologyPlant ScienceGeneral MedicineAscorbic acidPhotosynthesisPhotochemistryBiochemistrySuperoxide dismutaseCatalaseThylakoidbiology.protein

description

In a previous paper it was shown that photoinhibition of reaction centre II of spinach thylakoids was predominantly caused by the degradation of D1-protein. An initial inactivation step at the QB-site was distinguished from its breakdown. The present paper deals with the question as to whether this loss of QB-function is caused by oxygen radical attack. For this purpose the photoinhibition of thylakoids was induced at 20°C in the presence of either superoxide dismutase and catalase or the antioxidants glutathione and ascorbic acid. This resulted in comparable though not total protection of D1-protein, photochemistry and fluorescence from photoinhibition. The combined action of both the enzymatic and the non-enzymatic radical scavenging systems brought about an even more pronounced protective effect against photoinhibition than did either of the two systems singularly at saturating concentrations. The results signify a major contribution of activated oxygen species to the degradation process of D1-protein and the related phenomena of photoinhibition. Thylakoids treated with hydroxyl radicals generated through a Fenton reaction showed a loss of atrazine binding sites, electron transport capacity and variable fluorescence in a similar manner, though not to the same extent, as usually observed following photoinhibitory treatment.

10.1007/bf00032311https://pubmed.ncbi.nlm.nih.gov/24420076