ArticleThe journal of physical chemistry. B2014
Putative hydrogen bond to tyrosine M208 in photosynthetic reaction centers from Rhodobacter capsulatus significantly slows primary charge separation.
Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- On the unidirectionality of electron transfer in reaction centers of Chloroflexus aurantiacus.Photosynthesis research · 2026Article
- Inter-cofactor protein remodeling rewires short-circuited transmembrane electron transfer.Communications chemistry · 2025Article
- Primary charge separation in Chloroflexus aurantiacus reaction centers at room temperature: ultrafast transient absorption measurements on QPhotosynthesis research · 2025Article
- Contribution of Protonation to the Dielectric Relaxation Arising from Bacteriopheophytin Reductions in the Photosynthetic Reaction Centers ofBiomolecules · 2024Article
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- Photosynthetic reaction center variants made via genetic code expansion show Tyr at M210 tunes the initial electron transfer mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Pigment-modified reaction centers of Chloroflexus aurantiacus: chemical exchange of bacteriopheophytins with plant-type pheophytins.Photosynthesis research · 2021Article
- Switching sides-Reengineered primary charge separation in the bacterial photosynthetic reaction center.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Consequences of saturation mutagenesis of the protein ligand to the B-side monomeric bacteriochlorophyll in reaction centers from Rhodobacter capsulatus.Photosynthesis research · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
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Abstract
Slow, ∼50 ps, P* → P(+)HA(-) electron transfer is observed in Rhodobacter capsulatus reaction centers (RCs) bearing the native Tyr residue at M208 and the single amino acid change of isoleucine at M204 to glutamic acid. The P* decay kinetics are unusually homogeneous (single exponential) at room temperature. Comparative solid-state NMR of [4'-(13)C]Tyr labeled wild-type and M204E RCs show that the chemical shift of Tyr M208 is significantly altered in the M204E mutant and in a manner consistent with formation of a hydrogen bond to the Tyr M208 hydroxyl group. Models based on RC crystal structure coordinates indicate that if such a hydrogen bond is formed between the Glu at M204 and the M208 Tyr hydroxyl group, the -OH would be oriented in a fashion expected (based on the calculations by Alden et al., J. Phys. Chem. 1996, 100, 16761-16770) to destabilize P(+)BA(-) in free energy. Alteration of the environment of Tyr M208 and BA by Glu M204 via this putative hydrogen bond has a powerful influence on primary charge separation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.