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4. Environmental pH and a Glu364 to Gln mutation in the chlorophyll-binding CP47 protein affect redox-active TyrD and charge recombination in Photosystem II.

Author

Morris JN, Kovács S, Vass I, Summerfield TC, and Eaton-Rye JJ

Subjects
Glutamic Acid metabolism, Glutamine metabolism, Hydrogen Bonding, Hydrogen-Ion Concentration, Light-Harvesting Protein Complexes genetics, Models, Molecular, Oxidation-Reduction, Photosystem II Protein Complex genetics, Protein Binding, Synechocystis genetics, Tyrosine metabolism, Amino Acid Substitution, Chlorophyll metabolism, Light-Harvesting Protein Complexes chemistry, Light-Harvesting Protein Complexes metabolism, Photosystem II Protein Complex chemistry, Photosystem II Protein Complex metabolism, Synechocystis metabolism
Abstract

In Photosystem II, loop E of the chlorophyll-binding CP47 protein is located near a redox-active tyrosine, Y D , forming a symmetrical analog to loop E in CP43, which provides a ligand to the oxygen-evolving complex (OEC). A Glu364 to Gln substitution in CP47, near Y D , does not affect growth in the cyanobacterium Synechocystis sp. PCC 6803; however, deletion of the extrinsic protein PsbV in this mutant leads to a strain displaying a pH-sensitive phenotype. Using thermoluminescence, chlorophyll fluorescence, and flash-induced oxygen evolution analyses, we demonstrate that Glu364 influences the stability of Y D and the redox state of the OEC, and highlight the effects of external pH on photosynthetic electron transfer in intact cyanobacterial cells., (© 2018 Federation of European Biochemical Societies.)

Published
2019
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