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phylloquinone/spinacia oleracea

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Forward electron transfer from phylloquinone A1 to iron-sulfur centers in spinach photosystem I.

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Forward electron transfer at room temperature from the secondary acceptor A1 (phylloquinone) to the iron-sulfur centers FX, FB, and FA was studied by flash-absorbance spectroscopy in different photosystem I (PSI) preparations in order to resolve the controversy concerning the kinetics of
Leaf peroxisomes are fragile, low-abundance plant cell organelles that are difficult to isolate from one of the few plant species whose nuclear genome has been sequenced. Leaf peroxisomes were enriched at high purity from spinach (Spinacia oleracea) and approximately 100 protein spots identified
In our previous study, an antimutagenic compound from spinach (Spinacea oleracea L.), ethoxy-substituted phylloquinone (ESP) was isolated and characterized. The current study deals with elucidation of the possible mechanism of antimutagenicity of ESP against ethyl methanesulfonate (EMS) deploying
During in vitro analysis, spinach (Spinacea oleracea L.) leaf extracts displayed varying antimutagenicity when analyzed in models including human lymphoblast (TK+/-) cell line (thymidine kinase gene mutation assay) and Escherichia coli MG1655 (rifampicin resistance assay) against chemically (ethyl
Ionizing radiation of fruits and vegetables, in the form of gamma rays or electron beams, is effective in overcoming quarantine barriers in trade and prolonging shelf life, but a void of information persists on ionizing radiation effects of vitamin profiles in individual foods. Baby-leaf spinach

Site of prenylation reaction in synthesis of phylloquinone (vitamin K1) by spinach chloroplasts.

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One-carbonyl quinonoid compounds, fluorenone (fluoren-9-one), anthrone, and their derivatives are introduced into spinach photosystem (PS) I reaction centers in place of the intrinsic secondary electron acceptor phylloquinone (= vitamin K1). Anthrone and 2-nitrofluorenone fully mediated the

Electron transfer reactions of redox cofactors in spinach photosystem I reaction center protein in lipid films on electrodes.

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Thin film voltammetry was used to obtain direct, reversible, electron transfer between electrodes and spinach Photosystem I reaction center (PS I) in lipid films for the first time. This reaction center (RC) protein retains its native conformation in the films, and AFM showed that film structure

Comparison of phylloquinone bioavailability from food sources or a supplement in human subjects.

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Phylloquinone (K) absorption was assessed in 22- to 30-y-old human subjects consuming a standard test meal [402 kcal (1682 kJ), 27% energy from fat]. The absorption of phylloquinone, measured over a 9-h period as the area under the curve (AUC), was higher (P < 0.01) after the consumption of a 500-
Chlorophyll (Chl) a', the C132-epimer of Chl a, is a constituent of the primary electron donor (P700) of Photosystem (PS) I of a thermophilic cyanobacterium Synechococcus (Thermosynechococcus) elongatus, as was recently demonstrated by X-ray crystallography. To determine whether PS I of oxygenic
Selected substituted 1,4-benzoquinones, 1,4-naphthoquinones, and 9,10-anthraquinones were investigated as possible replacement quinones in spinach photosystem I (PSI) preparations that had been depleted of endogenous phylloquinone by extraction with hexane/methanol. As a criterion for successful
The dissociation constants (Kd) between the phylloquinone-binding site (designated as the Q phi site) and 23 quinones and 2 quinonoid compounds were measured in spinach photosystem I reaction centers. Kd values were calculated from the dependency of the recovery of the flash-induced stable oxidation

Localization of prenylquinones in the envelope of spinach chloroplasts.

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The isolated and purified chloroplast envelope of spinach leaves contains, besides carotenoids, several prenylquinones as basic constituents: plastoquinone-9, phylloquinone K1, alpha-tocoquinone and the chromanol, alpha-tocopherol. The relative quinone and carotenoid composition of the envelope

Photoaffinity labeling of the phylloquinone-binding polypeptides by 2-azidoanthraquinone in photosystem I particles.

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A photoaffinity label, 2-azido-9,10-anthraquinone, binds at the quinone-binding (Q phi) site with high affinity and can substitute for the secondary acceptor, phylloquinone, in photosystem I reaction center of spinach. Phylloquinone-depleted photosystem I particles reconstituted with
An unknown peak was observed in spinach extract during routine analysis of 7 pyrethroid insecticides by gas chromatography with electron capture detection (GC-ECD) using a DB-1 column (20 m x 0.25 mm id, 0.1 micron film thickness). It eluted later than the 7 pyrethroids, and it was also found in
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