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F F Litvin

Publications and source records attributed to F F Litvin.

At least 19 recordsLinked to original sources

Biosynthesis of chlorophyll from protochlorophyll(ide) in green plant leaves.

Using spectral methods, the biosynthesis of protochlorophyll(ide) and chlorophyll(ide) in green plant leaves was studied. The main chlorophyll precursors in the green leaves (as in etiolated leaves) were photoactive photocholorophyll(ide) forms Pchl(ide)655/650(448) and Pchl(ide)653/648(440). The contributions into Chl biosynthesis of the shorter-wavelength precursor forms, which were accumulated in darkened green leaves as well, were completely absent (of Pchl(ide) 633/628(440)) or insignificant (of Pchl(ide) 642/635(444)).

Chlorophyll↗

Biosynthesis of chlorophyll of photosystem II reaction centers in plant leaves in early stages of etiolation.

Spectral methods were used to study the sequences of chlorophyll biosynthesis reactions in etiolated pea, bean, and maize plants in early stages (3-4 days) of growth. For these juvenile plants, along with the reaction chain known for mature (7-9 day-old) plants, a new reaction chain was found which started with phototransformation of the long-wavelength form PChld 686/676 into PChld 653/648. (PChld 653/648 differs from the main known precursor form PChld 655/650). The subsequent photoreduction of PChld 653/648 leads to the formation of Chld 684/676, which is transformed into Chl 688/680 in the course of a dark reaction. After completion of this reaction, fast (20-30 sec) quenching of the fluorescence of the reaction product is observed with the formation of non-fluorescent Chl 680. The reaction accompanied by pigment fluorescence quenching is absent in pea mutants with depressed function of Photosystem II reaction centers. This suggests that the newly found reaction chain leads to the formation of chlorophyll of the Photosystem II reaction center.

Chlorophyll↗

Participation of free radicals in photoreduction of protochlorophyllide to chlorophyllide in an artificial pigment-protein complex.

The primary stages of protochlorophyllide phototransformation in an artificially formed complex containing heterologously expressed photoenzyme protochlorophyllide-oxidoreductase (POR), protochlorophyllide, and NADPH were investigated by optical and ESR spectroscopy. An ESR signal (g = 2.002; H = 1 mT) appeared after illumination of the complex with intense white light at 77 K. The ESR signal appeared with simultaneous quenching of the initial protochlorophyllide fluorescence, this being due to the formation of a primary non-fluorescent intermediate. The ESR signal disappeared on raising the temperature to 253 K, and a new fluorescence maximum at 695 nm belonging to chlorophyllide simultaneously appeared. The data show that the mechanism of protochlorophyllide photoreduction in the complex is practically identical to the in vivo mechanism: this includes the formation of a short-lived non-fluorescent free radical that is transformed into chlorophyllide in a dark reaction.

Chlorophyll↗

Nonpigment components of the photochlorophyllide photoactive complex: studies of low-temperature blue-green fluorescence spectra.

Fluorescence spectra in the blue-green region and excitation fluorescence spectra of green wheat leaves, etiolated wheat leaves and isolated inner etioplast membranes (prolamellar bodies and prothylakoids) were compared to specify the structure of the active protochlorophyllide pigment-protein complex of inner etioplast membranes. Three bands in the blue region at 420, 443 and 470 nm and a broader green band at 525 nm were found. Comparison of the emission and excitation spectra suggests that the main components responsible for the blue fluorescence of etioplast inner membranes are pyridine nucleotides and pterins. The green fluorescence (525 nm) excitation spectra of etiolated samples were identical to the excitation spectrum of flavin fluorescence. The fact confirms the suggestion that flavins are the constituents of the active protochlorophyllide-protein complex.

Chlorophyll↗

The final stage of chlorophyll biosynthesis and formation of reaction centres of photosystems.

The survey reviews Russian studies of the final stage of chlorophyll biosynthesis and the role of A. A. Krasnovsky (Sr.) in the development of this direction. The current state of the problem is considered. The results of studies carried out by Krasnovsky's followers at Moscow State University are summarized. Schemes of the pathways of chlorophyll and pheophytin biosynthesis, biogenesis of pigment complexes of the two photosystems of photosynthesis proposed by those scientists are presented.

Chlorophyll↗

The N intermediate of bacteriorhodopsin at low temperatures: stabilization and photoconversion.

In aqueous suspensions of purple membranes (pH 10.2, 0.4 M KCl) an intermediate having an absorption maximum at 570-575 nm (at -196 degrees C) was produced by first heating the M intermediate up to -30 degrees C and then stabilizing it by subsequent cooling to -60 degrees C. We suggest that this species is the intermediate N (or P or R) found and characterized earlier near room temperature. Upon illumination at -196 degrees C N is transformed into a bathochromically absorbing species KN which has an absorption maximum near 605 nm and an extinction 1.35 times that of N. This light reaction is photoreversible. The quantum yield ratio for the forward and back reaction is 0.18 +/- 0.02. The maximum photo steady state concentration of KN is about 0.24. The N intermediate was also trapped in water suspensions of purple membranes at neutral pH and low salt concentration by illumination at lambda greater than 620 nm during cooling. In addition to N another intermediate absorbing in the red (maximum at 610-620 nm) was accumulated in smaller amounts. It is not photoactive at -196 degrees C and apparently is the O intermediate or a photoproduct of N.

Bacteriorhodopsins↗

[Light-induced changes in quantum yields of the photochemical cycle of conversion of bacteriorhodopsin and transmembrane proton transfer in cells of Halobacterium halobium].

It was found that the rate of proton efflux from the cells, vH+, and the turnover number of bacteriorhodopsin photoconversion cycle per second, vM, are gradually decreased during continuous illumination of Halobacterium halobium with orange light (550-650 nm, 10(3) W/m2). The steady-state value of vH+ after 3 min of illumination is 3 times lower than vH+ at the 1st second of illumination. At the same time the concentration of the photochemical cycle intermediate, M412, the quantum yield of its formation, phi M, and the quantum efficiency of proton efflux, phi H+, are decreased (phi M and phi H+ up to 3-4-fold), whereas the concentration of the initial form of bacteriorhodopsin, BR570, and lifetime of M412, tau, are increased. These light-induced effects are abolished by uncoupler, carbonylcyanide m-chlorophenylhydrazone (CCCP) and are enhanced by the phosphorylation inhibitor, N,N'-dicyclohexylcarbodiimide (DCCD). This suggests that the observed changes of M412 and BR570 concentrations, tau, VH+, VM, phi M and phi H+ are due to the light-induced changes in the transmembrane electric potential, delta psi, and in pH inside and outside the cell, which control the photochemical cycle reactions. The decrease of phi M and phi H+ is discussed on the basis of an earlier proposed scheme of the branched photochemical cycle. It is assumed that the back reactions of the cycle (shunts) not coupled with the transmembrane proton translocation, e.g. conversion of L550 (P550) into BR570 without M412 formation, etc., become more probably at high values of the proton electrochemical potential gradient.

Bacteriorhodopsins↗

Photoinduction kinetics of electrical potential in a single chloroplast as studied with micro-electrode technique.

1. Using single chloroplasts of Peperomia metallica the kinetics of light-induced potential changes were studied. Three kinetic components (the initial fast rise, the decay in the light and the decay in the dark) were found to be characterized by time constants 4, 220 and 60 ms, respectively at light intensity 5000 1x and temperature 18 degrees C. After flash excitation the potential kept on rising for about 10 ms. Cooling of the medium down to 5 degrees C had no effect on the duration of potential rise after the flash. 2. Variations in the medium temperature in the range 2-23 degrees C had little effect on photoresponse magnitude but resulted in significant acceleration of decay in the light. 3. Addition of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (5-)0(-6) M) resulted in suppression of the magnitude of the photoresponse but was not accompanied by any change in the rate of initial rise of potential. 3-(3,4-Dichlorophenyl)-1,1-dimethylurea-inhibited photoresponse could be restored and even enhanced by subsequent addition of N-methylphenazonium methosulfate (10(-4) M). N-Methylphenazonium methosulfate essentially influenced the time course and light-intensity curves of photoresponse. 4. The chloroplast photoresponses were of different time-courses when elicited by red (640 nm) or far red (712 nm) light. This fact as well as an enhancement effect of combined illumination by two intermittent light beams indicate on the interaction of two photosynthetic pigment systems when the photoelectric response was formed. 5. An imposed electrical field resulted in stimulation or suppression of chloroplast photoresponse depending on the polarity of the field. No indications for the existance of "reversal potential" for photoelectric response were obtained. 6. A kinetic scheme of photoresponse formation is proposed, which includes two sequential photochemical reactions of photosynthesis.

Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone↗