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Construction and characterization of a photosystem II D1 mutant (arginine-269-glycine) of Chlamydomonas reinhardtii. 1996

R S Hutchison, and J Xiong, and R T Sayre, and Govindjee
Department of Biochemistry, Ohio State University, Columbus 43210, USA.

Numerous lines of evidence indicate that bicarbonate anion regulates electron and proton transfer processes in the photosystem II (PSII) complex of chloroplasts and cyanobacteria. On the reducing side of PSII, the addition of bicarbonate to bicarbonate-depleted (or formate-treated) membranes accelerates, especially, QA(-)-->QB(-) electron transfer kinetics. The site(s) at which bicarbonate binds is unknown. It is evident, however, from several spectroscopic studies that the bicarbonate binding site on the reducing side of PSII includes the non-heme iron located between the QA and QB sites. Since small anions may displace bicarbonate (Good, N.E. (1963) Plant Physiol. 38, 298-304) [1], it is apparent that the bicarbonate binding site is electrostatic in nature, presumably also involving positively charged amino acid residues. Previously, it had been predicted that residue arginine 269 of the PSII D1 protein may participate in bicarbonate binding. To test this hypothesis, we have generated a non-conservative mutation in the psbA gene of Chlamydomonas reinhardtii which converts residue R269 to a glycine (R269G). The R269G mutant was unable to grow photosynthetically or evolve oxygen. This phenotype is associated with a lack of the tetra-manganese water splitting complex and a reduced capacity to form a stabilized charge separated state (defined as TyrD+/QA- under the experimental conditions measured). In addition, the mutant cells have a less stable PSII complex than wild-type cells, particularly when grown in the light. It is apparent from analyses of the effect of formate on the magnitude of the QA-Fe+2 EPR signal, however, that the bicarbonate or formate binding site is not substantially affected by the R269G mutation. Although our results do not substantiate that residue R269 is the site at which bicarbonate is bound, they demonstrate the importance of R269 in the structure and function of PSII. It is apparent from analysis of the photosynthetic phenotype, that the structural perturbations on the stromal side of the D1 protein are transduced to the lumenal side of the membrane altering charge accumulating processes on the electron donor side of PSII.

UI MeSH Term Description Entries
D005998 Glycine A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter. Aminoacetic Acid,Glycine, Monopotassium Salt,Glycine Carbonate (1:1), Monosodium Salt,Glycine Carbonate (2:1), Monolithium Salt,Glycine Carbonate (2:1), Monopotassium Salt,Glycine Carbonate (2:1), Monosodium Salt,Glycine Hydrochloride,Glycine Hydrochloride (2:1),Glycine Phosphate,Glycine Phosphate (1:1),Glycine Sulfate (3:1),Glycine, Calcium Salt,Glycine, Calcium Salt (2:1),Glycine, Cobalt Salt,Glycine, Copper Salt,Glycine, Monoammonium Salt,Glycine, Monosodium Salt,Glycine, Sodium Hydrogen Carbonate,Acid, Aminoacetic,Calcium Salt Glycine,Cobalt Salt Glycine,Copper Salt Glycine,Hydrochloride, Glycine,Monoammonium Salt Glycine,Monopotassium Salt Glycine,Monosodium Salt Glycine,Phosphate, Glycine,Salt Glycine, Monoammonium,Salt Glycine, Monopotassium,Salt Glycine, Monosodium
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001120 Arginine An essential amino acid that is physiologically active in the L-form. Arginine Hydrochloride,Arginine, L-Isomer,DL-Arginine Acetate, Monohydrate,L-Arginine,Arginine, L Isomer,DL Arginine Acetate, Monohydrate,Hydrochloride, Arginine,L Arginine,L-Isomer Arginine,Monohydrate DL-Arginine Acetate
D016297 Mutagenesis, Site-Directed Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion. Mutagenesis, Oligonucleotide-Directed,Mutagenesis, Site-Specific,Oligonucleotide-Directed Mutagenesis,Site-Directed Mutagenesis,Site-Specific Mutagenesis,Mutageneses, Oligonucleotide-Directed,Mutageneses, Site-Directed,Mutageneses, Site-Specific,Mutagenesis, Oligonucleotide Directed,Mutagenesis, Site Directed,Mutagenesis, Site Specific,Oligonucleotide Directed Mutagenesis,Oligonucleotide-Directed Mutageneses,Site Directed Mutagenesis,Site Specific Mutagenesis,Site-Directed Mutageneses,Site-Specific Mutageneses
D016825 Chlamydomonas reinhardtii A species of GREEN ALGAE. Delicate, hairlike appendages arise from the flagellar surface in these organisms. Chlamydomonas reinhardii,Chlamydomonas reinhardius,Chlamydomonas reinhardtius,reinhardius, Chlamydomonas,reinhardtii, Chlamydomonas
D045322 Photosynthetic Reaction Center Complex Proteins Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II. Photosynthetic Complex,Photosynthetic Reaction Center,Photosynthetic Reaction Center Complex Protein,Photosynthetic Complexes,Photosynthetic Reaction Centers,Center, Photosynthetic Reaction,Complex, Photosynthetic,Complexes, Photosynthetic,Reaction Center, Photosynthetic,Reaction Centers, Photosynthetic
D045332 Photosystem II Protein Complex A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN. Chloroplast Reaction Center Protein D1,D1 Photosystem II Protein, Plant,Light-Induced D1 Protein, Photosystem II,Oxygen Evolving Enzyme,PRCP II D2 Protein,Photosystem II,Photosystem II Reaction Center,Photosystem II Reaction Center Complex D1 Protein,Photosystem II Reaction Center Complex D2 Protein,RCII-D1 Protein,Water Oxidase,Water-Splitting Enzyme of Photosynthesis,Enzyme, Oxygen Evolving,Evolving Enzyme, Oxygen,Light Induced D1 Protein, Photosystem II,Oxidase, Water,Photosynthesis Water-Splitting Enzyme,Water Splitting Enzyme of Photosynthesis

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