Photoinduced Fluorescence of Phylloquinone (Vitamin K1) in Solution.

Jansson, Owe

doi:10.3891/acta.chem.scand.24-2839

Cited by 11 publications

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“…Very similar biphasic kinetics have been reported by Lichtenthaler and Tevini [19] for spinach thylakoids for light of 254 nm. Since this short-wavelength UV light should be absorbed equally by both oxidized and reduced forms of the naphthoquinone (see spectra in [20]), it is unlikely that the biphasic kinetics are due to dif- ferent redox states of the quinone molecules in the precisely [23], i.e. the altered naphthoquinone may membranes.…”

Section: Resultsmentioning

confidence: 99%

Bound electron acceptors of photosystem I Evidence against the identity of redox center A₁with phylloquinone

1987

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Photosystem (PS) I preparations from spinach and from a cyanobacterium contain two molecules of phylloquinone (2-methyl-3-phytyl-1,4_naphthoquinone) per photosystem, only one of which is rapidly destroyed by ultraviolet light. In preparations of the core of PS I, the P700 reaction center, both quinone molecules are rapidly destroyed by UV irradiation. Nearly complete destruction does not alter the shape and size of the EPR spectrum of the electron acceptor A,, which is believed to be phylloquinone. Photooxidation of P700, the primary electron donor of PS I, is also not affected. The results provide strong evidence against the identity of redox center A, with the naphthoquinone.

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Section: Resultsmentioning

confidence: 99%

Bound electron acceptors of photosystem I Evidence against the identity of redox center A₁with phylloquinone

1987

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“…A calibration curve for the fluorometric determination of phylloquinone is shown in Figure 1. Plastoquinone-9 which was present in the samples did not contribute to the fluorescence emission (Jansson 1970).…”

Section: Experimental /mentioning

confidence: 85%

“…The concentration of phylloquinone was determined by irradiating the samples with the 365 nm mercury ling and measuring the highest fluorescence intensity at 431 nm as described in a previous paper (Jansson 1970). Irradiation and fluorescence measurements were made with a Zeiss spectrophotometer PMQ II connected with its fluorescence attachment ZFM 4.…”

Section: Experimental /mentioning

confidence: 99%

Effect of Menadiol Disulfate on the Phylloquinone Content of Wheat (Triticum aestivum)

Jansson

1972

Physiologia Plantarum

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Seedlings of Triticum aestivum L. were sprayed with menadiol disulfate in water solution. Eight days after spraying, the content of phylloquinone in the shoots was more than twice as high as in shoots of untreated control plants. The application of menadiol disulfate caused a stimulation of the synthesis of phylloquinone. It is possible that menadiol is an intermediate in the biosynthesis of phylloquinone.

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“…The green fluorescence, which is typical for K vitamins, was used for a semi-quantitative K, estimation (0.1-2 ^g) when compared with the fluorescence of an extra plate with spots of known K, concentrations. K, has also been determined in solution, making use of its green fluorescence in UV-light (Jansson 1970). After onedimensional TLC separation, the band, containing PQ-9 and Kj, was scratched off the plate, eluted in a quartz cuvette, irradiated in ethanol solution with UV-light (254 or 356 nm) until maximal green fiuorescence developed (c, 5-10 min, sensitivity 0.1-10 /ug).…”

Section: Chromatography Of Lipoquinonesmentioning

confidence: 99%

Determination of Prenylquinones in Green Photosynthetically Active Moss and Liver Moss Tissues

Lichtenthaler

Karunen

Grumbach

1977

Physiologia Plantarum

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The prenylquinone composition of two species of mosses (Polytrichum formosum Hedw., Sphagnum acutifoiium Ehrh.) and two species of liver mosses (Lumdaria cruciata (L.) Dum., Peilia epiphylla (L.) Cord.) was determined and compared with the chlorophyll content and the photosynthetic activity of the intact moss and liver moss tissues. 1. Green moss and liver moss tissues possess in principle the same prenylquinone composition as higher plants with plastoquinone-9, n-tocopherol, (t-tocoquinone and the phylloquinone K, as main components. On a chlorophyll basis the lipoquinone levels are lower than in higher plants. Differences among the individual mosses as well as within one species only occur in the quantitative levels of the chloroplast prenylquinones, but there are no differences between musci and liver mosses. 2. There are differences in the maximal fiuorescence of liver mosses and mosses. The variable fluorescence in tum, which is a measure of in vivo photosynthetic activity, is very similar for all examined species of mosses and liver mosses (values from 0.7 to 1.0) but somewhat lower than in leaf pieces of higher plants. DCMU blocks the variable fluorescence and the concomitant oxygen evolution in all mosses and liver mosses. 3. From the lower prenylquinone levels and the low values for the variable fiuorescence it is concluded that mosses and liver mosses exhibit on a chlorophyll basis fewer reaction centres and electron transport chains than chloroplasts of higher plants.

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Photoinduced Fluorescence of Phylloquinone (Vitamin K1) in Solution.

Cited by 11 publications

References 0 publications

Bound electron acceptors of photosystem I Evidence against the identity of redox center A₁with phylloquinone

Bound electron acceptors of photosystem I Evidence against the identity of redox center A₁with phylloquinone

Effect of Menadiol Disulfate on the Phylloquinone Content of Wheat (Triticum aestivum)

Determination of Prenylquinones in Green Photosynthetically Active Moss and Liver Moss Tissues

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Photoinduced Fluorescence of Phylloquinone (Vitamin K1) in Solution.

Cited by 11 publications

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Bound electron acceptors of photosystem I Evidence against the identity of redox center A1with phylloquinone

Bound electron acceptors of photosystem I Evidence against the identity of redox center A1with phylloquinone

Effect of Menadiol Disulfate on the Phylloquinone Content of Wheat (Triticum aestivum)

Determination of Prenylquinones in Green Photosynthetically Active Moss and Liver Moss Tissues

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Bound electron acceptors of photosystem I Evidence against the identity of redox center A₁with phylloquinone

Bound electron acceptors of photosystem I Evidence against the identity of redox center A₁with phylloquinone