pheophytin a/spanac

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Chromatographic determination of changes in pigments in spinach (Spinacia oleracea L.) during processing.

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The content of individual chlorophyll and carotenoid pigments is determined in three spinach varieties (Lorelei, Springfield, and Ballet) after processing. Raw spinach and spinach that is steam-blanched for 3, 9, or 15 min is stored frozen at -24 degrees C for 6 months. In addition, spinach is

D1-D2 complex of the photosystem II reaction center from spinach. Isolation and partial characterization.

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A pigment-protein complex consisting of D1 and D2 proteins, but depleted in the two lower molecular mass components of photosystem II, i.e. cytochrome b-559 and psbI gene product, has been isolated by octyl-beta-D-glucopyranoside treatment of the purified photosystem II reaction center complex from

Characterization of a D1-D2-cyt b-559 complex containing 4 chlorophyll a/2 pheophytin a isolated with the use of MgSO4.

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A D1-D2-cyt b-559 complex containing 4 chlorophyll alpha, 1 beta-carotene and 1 cytochrome b-559 per 2 pheophytin a has been isolated from spinach with 30% yield using a Q-Sepharose Fast-Flow anion-exchange column equilibrated with 0.1% Triton X-100, 10 mM MgSO4 and 50 mM Tris-HCl (pH 7.2). The

Identification and characterization of matrix components in spinach during QuEChERS sample preparation for pesticide residue analysis by LC-ESI-MS/MS, GC-MS and UPLC-DAD.

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In this article matrix components in spinach were investigated in detail. The samples were prepared using two QuEChERS (quick, easy, cheap, effective, rugged and safe) methods, AOAC and CEN. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS), gas

Determination of the primary charge separation rate in isolated photosystem II reaction centers with 500-fs time resolution.

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We have measured directly the rate of formation of the oxidized chlorophyll a electron donor (P680(+)) and the reduced electron acceptor pheophytin a(-) (Pheoa(-)) following excitation of isolated spinach photosystem II reaction centers at 4 degrees C. The reaction-center complex consists of D(1),

Key cofactors of photosystem II cores from four organisms identified by 1.7-K absorption, CD and MCD.

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Active Photosystem II (PS II) cores were prepared from spinach, pea, Synechocystis PCC 6803, and Thermosynechococcus vulcanus, the latter of which has been structurally determined [Kamiya and Shen (2003) Proc Natl Acad Sci USA 100: 98-103]. Electrochromic shifts resulting from QA reduction by 1.7-K

Energy dissipation in photosynthesis: does the quenching of chlorophyll fluorescence originate from antenna complexes of photosystem II or from the reaction center?

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Dissipation of light energy was studied in the moss Rhytidiadelphus squarrosus (Hedw.) Warnst., and in leaves of Spinacia oleracea L. and Arabidopsis thaliana (L.) Heynh., using chlorophyll fluorescence as an indicator reaction. Maximum chlorophyll fluorescence of

Chlorophyll a fluorescence lifetime distributions in open and closed photosystem II reaction center preparations.

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We have measured the decay of chlorophyll a fluorescence at 4 degrees C under anaerobic conditions in stabilized photosystem II reaction center complex isolated from spinach, using multifrequency (2-400 MHz) cross-correlation phase fluorometry. Examination of our data shows that although the

Effects of acid and alkali on the light absorption, energy transfer and protein secondary structures of core antenna subunits CP43 and CP47 of photosystem II.

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The effects of acid and alkali treatment on the light absorption, energy transfer and protein secondary structure of the photosystem II core antenna CP43 and CP47 of spinach were investigated by the absorption spectra, fluorescence emission spectra and circular dichroism spectra. It has been found

Chemical modification of photosystem II core complex pigments with sodium borohydride.

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The reaction of the irreversible chemical reduction of the 13(1)-keto C=O group of pheophytin a (Pheo a) with sodium borohydride in reaction centers (RCs) of functionally active spinach photosystem II (PS II) core complexes was studied. Stable, chromatographically purified PS II core complex

Femtosecond photodichroism studies of isolated photosystem II reaction centers.

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Photosynthetic conversion of light energy into chemical potential begins in reaction center protein complexes, where rapid charge separation occurs with nearly unit quantum efficiency. Primary charge separation was studied in isolated photosystem II reaction centers from spinach containing 6

Characterization of the low-temperature triplet state of chlorophyll in photosystem II core complexes: Application of phosphorescence measurements and Fourier transform infrared spectroscopy.

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Phosphorescence measurements at 77 K and light-induced FTIR difference spectroscopy at 95 K were applied to study of the triplet state of chlorophyll a ((3)Chl) in photosystem II (PSII) core complexes isolated from spinach. Using both methods, (3)Chl was observed in the core preparations with doubly

Stoichiometric determination of pheophytin in photosystem II of oxygenic photosynthesis.

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Pheophytin and chlorophyll extracted from oxygen-evolving photosystem II particles, chloroplast thylakoids and cyanobacterial cells were separated by column chromatography with DEAE-Toyopearl, and quantitatively determined by spectrophotometry. The molecular ratio of chlorophyll a+b to pheophytin a

Isolation and spectral characterization of Photosystem II reaction center from Synechocystis sp. PCC 6803.

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We isolated highly-purified photochemically active photosystem (PS) II reaction center (RC) complexes from the cyanobacterium Synechocystis sp. PCC 6803 using a histidine-tag introduced to the 47 kDa chlorophyll protein, and characterized their spectroscopic properties. Purification was carried out

Pigment quantitation and analysis by HPLC reverse phase chromatography: a characterization of antenna size in oxygen-evolving photosystem II preparations from cyanobacteria and plants.

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Photosystem II, the photosynthetic water-oxidizing complex, can be isolated from both plants and cyanobacteria. A variety of methods have been developed for purification of this enzyme, which can be isolated in several functional and structural forms. Knowledge of the pigment content of photosystem

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