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• W2040572237 endingPage "11880" @default.
• W2040572237 startingPage "11874" @default.
• W2040572237 abstract "The stable tyrosine radical in photosystem II, YD*, has been studied by ESR and ENDOR spectroscopies to obtain proton hyperfine coupling constants from which the electron spin density distribution can be deduced. Simulations of six previously published ESR spectra of PSII (one at Q band; five at X band, of which two were after specific deuteration and two others were of oriented membranes) can be achieved by using a single set of magnetic parameters that includes anisotropic proton hyperfine tensors, an anisotropic g tensor, and noncoincident axis systems for the g and A tensors. From the spectral simulation of the oriented samples, the orientation of the phenol head group of YD* with respect to the membrane plane has been determined. A similar orientation for YZ*, the redox-active tyrosine in PSII that mediates electron transfer between P680 and the oxygen-evolving complex, is expected. ENDOR spectra of YD* in PSII preparations from spinach and Synechocystis support the set of hyperfine coupling constants but indicate that small differences between the two species exist. Comparison with the results of spectral simulations for tyrosyl radicals in ribonucleotide reductase from prokaryotes or eukaryotes and with in vitro radicals indicates that the spin density distribution remains that of an odd-alternant radical but that interactions with the protein can shift spin density within this basic pattern. The largest changes in spin density occur at the tyrosine phenol oxygen and at the ring carbon para to the oxygen, which indicates that mechanisms exist in the protein environment for fine-tuning the chemical and redox properties of the radical species." @default.
• W2040572237 created "2016-06-24" @default.
• W2040572237 creator A5020205401 @default.
• W2040572237 creator A5028940854 @default.
• W2040572237 date "1992-12-01" @default.
• W2040572237 modified "2023-10-14" @default.
• W2040572237 title "Protein-tyrosyl radical interactions in photosystem II studied by electron spin resonance and electron nuclear double resonance spectroscopy: comparison with ribonucleotide reductase and in vitro tyrosine" @default.
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• W2040572237 doi "https://doi.org/10.1021/bi00162a028" @default.
• W2040572237 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1332777" @default.
• W2040572237 hasPublicationYear "1992" @default.
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