[Technique for the determination of the quantum yield of the primary process in the course of photosynthesis energy transformation. III. Experimental data obtained for different photosynthetic organisms]. / Opredelenie kvantovogo vykhoda pervichnogo preobrazovaniia energii pri fotosintez III. Eksperimental'nye dannye dlia razlichnykh fotosinteziruiushchikh organizmov

A relative method in two modifications has been developed for determination of the quantum yield of primary photosynthesis energy conversion. The purple bacteria E. chaposhnikovii and Chr. minutissimum, R. rubrum chromatophores, cell extracts of E. shaposhnikovii, Rps. spheroides strains GA and R-26, pigment-protein complexes from green bacterium Chl. limicola and light subchloroplast particles, enriched in the photosystem I, were investigated. The quantum yields for all these objects were shown to be 90-98%. The accuracy of the relative method used is very high (within 2--4+). The photosynthetic units were proved to be of a multicentral type for all these systems. The quantum yield values permit estimation of the coefficient of efficiency of the primary conversion process as being approximately equal to 35-38% for bacteria and approximately equal to 50% plants.

[Shifts of the bacteriochlorophyll absorption band at 880 nm in chromatophores and subchromatophore pigment-protein complexes from Rhodospirillum rubrum]. / Sdvigi polosy pogloshcheniia bakteriokhlorofilla pri 880 nm v khromatoforakh i subkhromatofornykh pigment-belkovykh kompleksakh Rhodospirillum Rubrum.

The redox potential dependency of the light-induced absorption changes of bacteriochlorophyll in the chromatophores and subchromatophore particles from Rhodospirillum rubrum has been studied. The highest values of the absorption changes due to the bleaching of P870 and the blue shift of P800 are observed within the redox potential range of 360--410. At the potential values below 300 mV the 880 nm band of bacteriochlorophyll shifts to shorter wavelengths in the subchromatophore particles and to longer wavelengths in the chromatophores. Redox titration revealed that the red and blue shifts of 880 nm bacteriochlorophyll band are caused by the functioning of a non-identified component (X) which has an oxidation -- reduction midpoint potential close to 340 mV (n = 1) within the pH range of 6,0--7,6. The Em for this component decreases by 60 mV/pH unit within the pH range of 7.6--9,2. The results obtained suggest that the red shift is due to the transmembrane, while the blue shift -- to the local intramembrane electric field. The generation of both the transmembrane and local intramembrane electric fields apparently depends on redox transitions of the component X.

[Generation of the differences of the electric potentials by Rhodospirillum rubrum reaction center complexes devoid of the heavy subunit]. / Obrazovanie raznosti élektricheskikh potentsialov kompleksami reaktsionnykh tsentrov Rhodospirillum rubrum, lishennymi tiazheloi sub"edinitsy.

The electrogenic activity of Rhodospirillum rubrum P870 reaction center complexes devoid of the heavy (H) subunit and retaining the light (L) and medium (M) subunits, was studied. The proteoliposomes containing such reaction center complexes were formed by a self-assembly procedure, using soya bean phospholipids. In the presence of Ca2+ the reaction center proteoliposomes were incorporated into a phospholipid-impregnated Teflon filter separating two solutions of identical composition. After addition of N,N,N',N'-tetra-methyl-p-phenylenediamine (or cytochrome c) and qinone (menadione), illumination caused generation of an electric potential difference between the two filter-separated compartments, the proteoliposome-free compartment being negatively charged. The illuminated proteoliposomes took up penetrating tetraphenylphosphonium cations and, in a lesser degree, tetraphenylborate anions. The data obtained suggest that the reaction center complexes containing only L- and M-subunits possess the electrogenic activity. The H-subunit is not directly involved in membrane potential generation.

[Reconstruction of the function of membrane potential formation by isolated pigment-protein complexes of Rhodospirillum rubrum]. / Rekonstruktsiia funktsii obrazovaniia membrannogo potentsiala izolirovannymi pigment-belkovymi kompleksami Rhodospirillum rubrum

The pigment-protein complexes, containing the photosynthetic reaction centers and chlorophyll antenna, were isolated from non-sulfur purple bacteria Rhodospirillum rubrum, by use of cholate. Absorption spectra and quantum yield of photo-oxidation of bacteriochlorophyll P870 of complexes were similar to those of chromatophores. The procedure of reconstitution of proteoliposomes from phospholipids and complexes was proposed. The proteoliposomes incubated with CoQ6 and TMPD upon illumination are generating the transmembrane electric potential difference (plus inside proteoliposomes). The electric potential difference was registered by three independent methods: by transmembrane electrophoresis of penetrating anions PCB-, by direct measurement with using voltmeter in system "proteoliposome--planar membrane" and electrochromic absorption band shifts of bacteriochlorophyll.

[Photosynthetic oxygen evolution and CO2 photoassimilation by cyanobacteria that form water-bloom spots in a sulfur spring with a high sulfide content]. / Fotosinteticheskoe vydelenie kisloroda i fotoassimiliatsiia CO2 tsianobakteriiami, obrazuiushchimi piatna tsveteniia v sernom istochnike s vysokim soderzhaniem sul'fida.

Cyanobacteria belonging mainly to the genera Anabaena and Oscillatoria were isolated from water-bloom spots of a sulfur spring in Staraya Matsesta. Their suspensions evolved O2 at a rate of 6--8 nM/min per 1 mg of dry cell weight at an intensity of solar radiation being 60--75 mV/cm2 per 1 sec. The cells were also capable of CO2 photoassimilation in the presence of solfide at a rate of 10(-4) mg C per mg per hour. DCMU at a concentration of 10(-5) M completely inhibited O2 evolution and inhibited CO2 fixation by 80%. Oxygen assimilation in dark by the suspensions did not depend on the addition of cyanide and was caused apparently by nonenzymatic reduction of O2 with sulfide dissolved in the spring water. Oxygen assimilation by the suspensions in light in the presence of DCMU was by 20--30% greater than in dark. Therefore, the cells of cyanobacteria are characterized by photorespiration at the level of photosystem I. Presumably, sulfide at a concentration of 9 mM cannot significantly inhibit the photosynthetic processes in cyanobacteria producing water-bloom spots in the sulfur spring.

[The surface membrane charge of bacteria and its role in serine proteinase secretion by Bacillus subtilis cells]. / Poverkhnostnyi zariad membran bakterii i ego rol' v sekretsii serinovoi proteinazy kletkami Bacillus subtilis.

Univalent, bivalent and trivalent metal cations increase the fluorescence yield of 9-aminoacridine in the suspensions of chromatophores of the purple nonsulfur bacterium Rhodospirillum rubrum isolated thylakoid membranes and cells of cyanobacterium Anabaena variabilis, cells Bacillus subtilis. The active cation concentrations increase about in 10 times with the decrease of their valency by one. It points to the fact that the changes in 9-aminoacridine fluorescence serve for the monitoring of the surface charge of bacterial membranes. The negative surface charge of B. subtilis cells increases before the onset of the serine protease secretion. The metal cations stimulate the serine protease secretion by B. subtilis cells, the stimulating effect correlates with the action of cations on the 9-aminoacridine fluorescence yield. It is suggested that the surface charge of cytoplasmic membrane regulates the formation and release of serine protease by the cells of B. subtilis.