ArticleProceedings of the National Academy of Sciences of the United States of America2002
Functional asymmetry of photosystem II D1 and D2 peripheral chlorophyll mutants of Chlamydomonas reinhardtii.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 50 citations in OpenAlex.
- Structural basis of light-harvesting in the photosystem II core complex.Protein science : a publication of the Protein Society · 2020Review
- Development of fluorescence quenching in Chlamydomonas reinhardtii upon prolonged illumination at 77 K.Photosynthesis research · 2018Article
- Structure-Function Analysis of Chloroplast Proteins via Random Mutagenesis Using Error-Prone PCR.Plant physiology · 2018Article
- On the Conflicting Estimations of Pigment Site Energies in Photosynthetic Complexes: A Case Study of the CP47 Complex.Analytical chemistry insights · 2016Review
- Critical assessment of the emission spectra of various photosystem II core complexes.Photosynthesis research · 2015Article
- Dynamic protein conformations preferentially drive energy transfer along the active chain of the photosystem II reaction centre.Nature communications · 2014Article
- Picosecond spectroscopy of the isolated reaction centers from the photosystems of oxygenic photosynthesis--ten years (1987-1997) of fun : a tribute to Michael R. Wasielewski on his 60th birthday.Photosynthesis research · 2010Article
- Kinetics and mechanism of electron transfer in intact photosystem II and in the isolated reaction center: pheophytin is the primary electron acceptor.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Structure, function and assembly of Photosystem II and its light-harvesting proteins.Photosynthesis research · 2004Article
- Engineering the chloroplast encoded proteins of chlamydomonas.Photosynthesis research · 2004Article
- The isolated Photosystem II reaction center: first attempts to directly measure the kinetics of primary charge separation.Photosynthesis research · 2003Article
- What is beta-carotene doing in the photosystem II reaction centre?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2002Article
- Room temperature photooxidation of beta-carotene and peripheral chlorophyll in photosystem II reaction centre.Photosynthesis researchArticle
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peripheral accessory chlorophylls (Chls) of the photosystem II (PSII) reaction center (RC) are coordinated by a pair of symmetry-related histidine residues (D1-H118 and D2-H117). These Chls participate in energy transfer from the proximal antennae complexes (CP43 and CP47) to the RC core chromophores. In addition, one or both of the peripheral Chls are redox-active and participate in a low-quantum-yield electron transfer cycle around PSII. We demonstrate that conservative mutations of the D2-H117 residue result in decreased Chl fluorescence quenching efficiency attributed to reduced accumulation of the peripheral accessory Chl cation, Chl(Z)(+). In contrast, identical symmetry-related mutations at residue D1-H118 had no effect on Chl fluorescence yield or quenching kinetics. Mutagenesis of the D2-H117 residue also altered the line width of the Chl(Z)(+) EPR signal, but the line shape of the D1-H118Q mutant remained unchanged. The D1-H118 and D2-H117 mutations also altered energy transfer properties in PSII RCs. Unlike wild type or the D1-H118Q mutant, D2-H117N RCs exhibited a reduced CD doublet in the red region of Chl absorbance band, indicative of reduced energetic coupling between P680 and the peripheral accessory Chl. In addition, transient absorption measurements of D2-H117N RCs, excited on the blue side of the Chl absorbance band, exhibited a ( approximately 400 fs) pheophytin Q(X) band bleach lifetime component not seen in wild-type or D1-H118Q RCs. The origin of this component may be related to delayed fast-energy equilibration of the excited state between the core pigments of this mutant.
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