title: Mercury inhibition at the donor side of photosystem II is reversed by chloride.
abstract: Mercury is an environmental contaminant that strongly inhibits photosynthetic electron transport, photosystem II being the most sensitive target. We investigated in greater detail the effect of mercury using photosystem II submembrane fractions of higher plants. Oxygen evolution was strongly inhibited and variable chlorophyll fluorescence was severely quenched by mercury. Chloride, an inorganic cofactor known to be essential for the optimal function of photosystem II, significantly reversed the inhibitory effect of mercury. However, calcium, another essential cofactor, showed no reversal capacity. It is concluded that on the donor side of PSII, mercury exerts its action by perturbing chloride binding and/or function. Considering the exceptional affinity of mercury for sulfhydryl groups of proteins, the results suggest the implication of cystein residue(s) in maintaining structural and functional integrity of photosystem II.
authors: Centre de recherche en photobiophysique, Université du Québec, Trois-Rivières, Canada.
authors: M
authors: M
authors: Bernier
authors: R
authors: R
authors: Popovic
authors: R
authors: R
authors: Carpentier
mesh_terms: D002712:Chlorides / Q000494:pharmacology*; D003545:Cysteine / Q000037:antagonists & inhibitors / Q000502:physiology; D001467:Hordeum; D066298:In Vitro Techniques; D045342:Light-Harvesting Protein Complexes; D008628:Mercury / Q000037:antagonists & inhibitors*; D010788:Photosynthesis / Q000187:drug effects*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000037:antagonists & inhibitors*; D045332:Photosystem II Protein Complex; D013050:Spectrometry, Fluorescence
chemical_list: D002712:Chlorides; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D008628:Mercury; D003545:Cysteine