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spinacia inermis/tyrosine
Ο σύνδεσμος αποθηκεύεται στο πρόχειρο
Σελίδα 1 από 87 Αποτελέσματα
Formation of tyrosine radicals in photosystem II under far-red illumination.
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Photosystem II (PS II) contains two redox-active tyrosine residues on the donor side at symmetrical positions to the primary donor, P680. TyrZ, part of the water-oxidizing complex, is a preferential fast electron donor while TyrD is a slow auxiliary donor to P680+. We used PS II membranes from
Heat-induced changes in the EPR signal of tyrosine D (Y(D)OX) a possible role of Cytochrome b559.
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The present study for the first time describes a close relationship between a change in the states of Cyt b559, a damage to Mn complex and a rapid reduction of tyrosine D (Y(D)) as a function of temperature in spinach thylakoid membranes. Measurements of the EPR signal of dark stable tyrosine D in
The dark stable tyrosine radical of photosystem 2 studied in three species using ENDOR and EPR spectroscopies.
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The dark stable neutral tyrosine radical YD. of photosystem 2 (PS2) has been studied using electron nuclear double-resonance (ENDOR) and electron paramagnetic resonance (EPR) spectroscopies. The proton hyperfine coupling constants of all four ring protons and both beta-methylene protons have been
Water molecules coupled to the redox-active tyrosine Y(D) in photosystem II as detected by FTIR spectroscopy.
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The redox-active tyrosine YD (D2-Tyr160) in photosystem II (PSII) serves as a side-path electron donor to P680. When YD is oxidized, a proton is released from phenolic OH, and a neutral radical YD* is formed. A hydrogen bond network around YD must be deeply involved in the mechanism of the YD
Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II.
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Saturation-recovery EPR spectroscopy has been used to probe the location of the redox-active tyrosines, YD (tyrosine 160 of the D2 polypeptide, cyanobacterial numbering) and YZ (tyrosine 161 of the D1 polypeptide), relative to the non-heme Fe(II) in Mn-depleted photosystem II (PSII). Measurements
Photo processes on self-associated cationic porphyrins and plastocyanin complexes 1. Ligation of plastocyanin tyrosine 83 onto metalloporphyrins and electron-transfer fluorescence quenching.
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The spectroscopic properties of the self-associated complexes formed between the anionic surface docking site of spinach plastocyanin and the cationic metalloporphyrins, in which the tyrosine 83 (Y83) moiety is placed just below the docking site, tetrakis(N-methyl-4-pyridyl)porphyrin
A functional role for tyrosine-D in assembly of the inorganic core of the water oxidase complex of photosystem II and the kinetics of water oxidation.
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The role of D2-Tyr160 (Y(D)), a photooxidizable residue in the D2 reaction center polypeptide of photosystem II (PSII), was investigated in both wild type and a mutant strain (D2-Tyr160Phe) in which phenylalanine replaces Y(D) in the cyanobacterium Synechocystis sp. (strain PCC 6803). Y(D) is the
Generation, oxidation by the oxidized form of the tyrosine of polypeptide D2, and possible electronic configuration of the redox states S0, S-1, and S-2 of the water oxidase in isolated spinach thylakoids.
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Suitable treatment of thylakoids with hydrazine permits a high population of the redox states S0, S-1, and S-2 in the water oxidase. Experiments performed with dark-adapted samples enriched either in the oxidized or reduced form of the redox-active tyrosine, YD, of polypeptide D2 reveal that YoxD is
Fourier transform infrared difference spectroscopy of photosystem II tyrosine D using site-directed mutagenesis and specific isotope labeling.
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Tyrosine D (TyrD), a side path electron carrier of photosystem II (PS II), has been studied by light-induced Fourier transform infrared (FTIR) difference spectroscopy in PS II core complexes of Synechocystis sp. PCC 6803 using the experimental conditions previously optimized to generate the pure
A rare protein fluorescence behavior where the emission is dominated by tyrosine: case of the 33-kDa protein from spinach photosystem II.
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An abnormal fluorescence emission of protein was observed in the 33-kDa protein which is one component of the three extrinsic proteins in spinach photosystem II particle (PS II). This protein contains one tryptophan and eight tyrosine residues, belonging to a "B type protein". It was found that the
Tyrosine residues of the extrinsic 23 kDa protein are important for its interaction with spinach PSII membranes.
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The 1, 4, and 8 tyrosine (Tyr) residues on the PSII extrinsic 23 kDa protein were modified with 5, 10 or 40 mM N-acetylimidazole (NAI) respectively. The amount of rebound NAI-modified extrinsic 23 kDa protein was 98%, 80%, and 5% of that in the unmodified protein, respectively. These results
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.
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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
Probing tyrosine Z oxidation in Photosystem II core complex isolated from spinach by EPR at liquid helium temperatures.
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Tyrosine Z (Tyr(Z)) oxidation observed at liquid helium temperatures provides new insights into the structure and function of Tyr(Z) in active Photosystem II (PSII). However, it has not been reported in PSII core complex from higher plants. Here, we report Tyr(Z) oxidation in the S(1) and S(2)
Replacement of tyrosine D with phenylalanine affects the normal proton transfer pathways for the reduction of P680+ in oxygen-evolving photosystem II particles from Chlamydomonas.
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We have probed the electrostatics of P680(+) reduction in oxygenic photosynthesis using histidine-tagged and histidine-tagged Y(D)-less Photosystem II cores. We make two main observations: (i) that His-tagged Chlamydomonas cores show kinetics which are essentially identical to those of Photosystem
245 GHz high-field EPR study of tyrosine-D zero and tyrosine-Z zero in mutants of photosystem II.
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A 245 GHz 8.7 T high-field EPR study of tyrosine-D (TyrD zero) and tyrosine-Z (TyrZ zero) radicals of photosystem II (PSII) from Synechocystis PCC 6803 was carried out. Identical principal g values for the wild-type Synechocystis and spinach TyrD zero showed that the two radicals were in similar
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