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PubMed1983

[Dicyclohexylcarbodiimide as an inhibitor of light- and pyrophosphate-induced formation of membrane potential in chromatophores of purple bacteria].

N,N'-Dicyclohexylcarbodiimide (DCCD) suppresses the uptake of penetrating tetraphenylborate anions by Rhodospirillum rubrum chromatophores during cyclic and non-cyclic electron transfer and ATP and PP i hydrolyses. The photochemical activity of the bacteriochlorophyll reaction centers of the chromatophores in insensitive to DCCD. This supports the view that DCCD inhibits the electron transfer between the primary and secondary quinones of the photosynthetic chain. Incorporation of the chromatophores into a planar phospholipid-decane membrane abolishes or considerably reduces the inhibiting effect of DCCD on the membrane potential generation during the light-induced electron transfer and PP i (but not ATP) hydrolysis. The inhibition of the photosynthetic electron transfer is proposed to be due to the effect of DCCD as a quinone antagonist which competes with the secondary quinone for the binding at the active site. By expelling quinones DCCD seems to destroy the specific microenvironment of PPiase in the membrane and to inhibit its catalytic activity. In the system with the planar membrane decane and/or phospholipids remove the effect of DCCD as a quinone antagonist.

Bacterial Chromatophores↗

PubMedDate not supplied

[Linear dichroism of pigments associated with spherical chromatophores. Models of orientation in polyacrylamide gels].

Linear dichroism and orientation of pigments in chromatophores of photosynthetic bacteria Chromatium minutissimum and Rhodospirillum rubrum using a novel method of orientation in polyacrylamide gel was studied. A model is proposed for orientation of spherical membranes of chromatophores or other similar vesicules. The value of linear dichroism is derived for known deformation of the gel and a certain angle between the transition dipole and a unit vector perpendicular to the membrane plane. The analysis of linear dichroism spectra permits calculation of angles between the normal to the membrane and the transition dipoles in Chr. minutissimum 65 degrees +/- 1.5 degrees (890 nm absorption band), 63 degrees +/- 1 degree (860 nm), 63 degrees +/- 1 degree (800 nm), 45.5 degrees +/- 1 degree (590 nm), 50.5 degrees +/- 0.5 degree (450--550 nm) and in Rsp. rubrum: 71 degrees +/- 1.5 degree (890 nm), 66.5 degrees +/- 1 degree (870 nm), 69 degrees +/- 1.5 degree (800 nm), 37 degrees +/- 0.5 degree (590 nm), 49.5 degrees +/- 0.5 degree (450--550 nm). The 860 nm band shift to shorter wave-lengths observed in Chr. minutissimum chromatophores treated with 0.01 M potassium ferricyanide is not related to reorientation of transition dipoles, but rather to certain changes of lipid-protein environment.

Acrylic Resins↗

PubMed1980

[Cyclic electron transfer and membrane potential generation in chromatophores on non-sulfur bacteria Rhodospirillum rubrum].

The uptake of permeant anions by cells and chromatophores of the non-sulfur purple bacteria R. rubrum has been studied. Antimycin A causes biphasic inhibition of the light-induced uptake of tetraphenylborate anions (TB-) by the cells and the isolated chromatophores incubated under anaerobic conditions. The first phase is observed at small concentrations of antimycin and is due to its effect as an inhibitor of the cyclic electron transfer. The second phase is observed at concentrations higher than 1 microM and is due to its effect as an uncoupler of photophosphorylation. The inhibitory effect of antimycin is greatly enhanced under aerobic conditions and is due to its effect as an uncoupler of photophosphorylation. The innic cyclic redox chain in the isolated and intracellular chromatophores is apparently operated in two regimens: 1) as a chain including all redox components and, 2) as a chain functioning without cytochromes of the b type.

Antimycin A↗

PubMed1982

[Reversible effect of intensive light on photobiochemical properties of Rhodospirillum rubrum chromatophores].

The effect of high intensity (photosynthesis-saturating) light on the optical properties of the bacteriochlorophyll and the light-induced H+ uptake by R. rubrum chromatophores was studied. It was shown that under aerobic conditions illumination causes reversible inhibition (in the dark) of the chromatophore ability for the light-induced uptake of H+, a reversible inhibition of the photosynthetical reaction center function and irreversible bleaching of the antennal bacteriochlorophyll. A kinetic comparison of spectral effects and reversible changes in pH as well as the effects of atmospheric oxygen and exogenous electron donors suggests that inhibition of photoactivity of the chromatophores upon illumination is due to accumulation of oxidized bacteriochlorophyll in the reaction center.

Bacterial Chromatophores↗

PubMed1965

THE PHOTO-OXIDATION OF SUCCINATE BY CHROMATOPHORES OF RHODOSPIRILLUM RUBRUM.

1. The stoicheiometry of the photo-oxidation of succinate by chromatophores has been investigated with [2,3-(14)C(2)]succinate. It was found that there is a stoicheiometric relationship between the amount of succinate oxidized and the NAD reduced, and that fumarate is the only product of succinate oxidation. 2. The possibility of a direct hydrogen transfer from succinate to NAD in this reaction was investigated with tritiated substrates. With tritiated succinate less than 3% of the activity expected if direct hydrogen transfer occurred was recovered in the NADH(2), and this was due to contamination with the substrate. In experiments with tritiated water, NADH(2) was labelled, and had half the specific activity of the water, as expected if water was the source of protons. It was also found that chromatophores catalyse an exchange reaction between NADH(2) and water. 3. It is concluded that the exchange reaction makes it impossible to interpret these results as indicating either a hydrogen-transfer or an electron-transfer mechanism for the photoreduction reaction.

Bacterial Chromatophores↗

PubMed1964

THE PREPARATION AND PROPERTIES OF BACTERIAL CHROMATOPHORE FRACTIONS.

Chromatophore material from the bacterium Rhodopseudomonas spheroides was freed of ribosomes by centrifugation in 27 per cent RbCl and then separated into "heavy" and "light" fractions by centrifugation through a sucrose gradient. The fractions differed from one another in the following ways. (a) The isopycnic density of the heavy fraction was between 1.15 and 1.18 gm/ml and that of the light fraction was 1.14 gm/ml. (b) The heavy fraction was able to bind ribosomes; the light fraction was not. (c) The light fraction was homogeneous in the ultracentrifuge and had a sedimentation constant, extrapolated to infinite dilution, of 153 s(20,w). The heavy fraction was grossly heterogeneous. (d) Both the amount of bacteriochlorophyll relative to protein and the ratio of bacteriochlorophyll to carotenoids were greater in the light fraction. (e) The spectra of the two fractions in the near infra-red were different. Comparisons of the chromatophore fractions from cells with different amounts of bacteriochlorophyll showed that the specific bacteriochlorophyll contents of the two fractions did not change to the same extent as did that of the whole cells. The amount of heavy fraction from pigmented cells was roughly independent of the cellular pigment content and was about equal to that from pigment-free cells. The amount of light fraction depended on the pigment content of the cells; no light fraction was obtained from cells devoid of bacteriochlorophyll. The cytochrome complements of both fractions underwent quantitative as well as qualitative changes with varying growth conditions. The size of the photosynthetic unit in R. spheroides appeared to increase as the total cellular bacteriochlorophyll content increased; however, the number of units per light fraction particle remained constant.

Bacterial Chromatophores↗

PubMed1999

[Light-dependent incorporation of selenite into selenocysteine by isolated chromatophore of Chromatium vinosum].

Illiminated intact chromatophore of chromatium vinosum in the presence of O-acetylserine(OAS) catalysed incorporation of SeO3(2-) into selenocysteine at rate of 359 nmol.mgBchl-1.h-1. Sonicated chromatophore catalysed SeO3(2-) incorporation at 1.1% of the rate of intact chromatophore. Addition of GSH and NADPH increased the rate to 88.3% of intact rate, but SeO3(2-) incorporation under these conditions was essentially light dependent. The purified GSH reductase from Chromatium vinosum in the presence of cysteine synthase OAs and NADPH catalysed incorporation of SeO3(2-) into selenocysteine. It is proposed that SeO3(2-) is reduced by light-coupled GSH reductase and that Se2- produced is incorporated into selenocysteine by cysteine synthase.

Catalysis↗

PubMed1978

Ultrastructural changes in the dermal chromatophore unit of Hyla arborea during color change.

The structural changes in the chromatophores of Hyla arborea related to changes in skin color were studied by electron microscopy and reflectance microspectrophotometry. During a change form a light to a darker green color, the melanosomes of the melanophores disperse and finally surround the iridophores and partly the xanthophores. The iridophores change from cup-shape to a cylindrical or conical shape with a simultaneous change in the orientation of the platelets from being parallel to the upper surface of the iridophores to being more irregular. The xanthophores change from lens-shape to plate-shape. The color change from green to grey seems always to go through a transitional black-green or dark olive green to dark grey. During this change the xanthophores migrate down between the iridophores, and in grey skins they are sometimes found beneath them. The pterinosomes gather in the periphery of the cell, while the carotenoid vesicles aggregate around the nucleus. The iridophores in grey skin are almost ball-shaped with concentric layers of platelets. A lighter grey color arises from a darker grey by an aggregation of melanosomes. The chromatophore values previously defined for Hyla cinerea are applicable in Hyla arborea, and the ultrastructural studies support the assumptions previously made to explain these values.

Animals↗

PubMed1995

The ultrastructure and innervation of muscles controlling chromatophore expansion in the squid, Loligo vulgaris.

Squid chromatophores are organs of colour change, consisting of a pigment sac opened by contraction of 10-24 radial muscle fibres. The ultrastructure and innervation of these muscle fibres were examined by electron microscopy and diagramatic reconstructions made on the basis of serial ultra-thin sections. At the proximal end of the fibre, nearest the pigment sac a cortical myofilament zone surrounds 2 cores containing mitochrondria; further along the fibre these merge to form one central core. The myofilament zone forms a groove containing a nerve bundle consisting of 2 to 4 axons per muscle fibre. The axons are surrounded by glial cell processes, and either originate from a neighbouring fibre, or join the fibre at some point along its length. Axons twist around each other, forming a series of synapses with the muscle fibre. As many as 6-37 synapses exist along the length of each muscle fibre; the mean synapse interval is 9.05 microm, but the largest may be 123 microm. At the distal end of the muscles, the nerve is located towards the middle of the fibre, which it penetrates as the muscle splits up. Electron-lucent vesicles are present in all synaptic regions, but electron-dense vesicles are only found towards the distal end of the fibre. There is thus a possibility that more than one neurotransmitter is present in the nerves innervating chromatophores. Electron-lucent and dense-cored vesicles are not colocalised.

Actin Cytoskeleton↗

PubMed1981

Lateral organization of proteins in the chromatophore membrane of Rhodospirillum rubrum studied by chemical cross-linking.

The organization of proteins in the chromatophore membrane, particularly of the reaction center and the light-harvesting polypeptide, was examined by the use of a hydrophobic and a hydrophilic cross-linking reagent, namely DSP (dithiobis-succinimidyl propionate) and glutaraldehyde. The linkage of proteins was studied by SDS polyacrylamide pore gradient electrophoresis. DSP was shown to link proteins within the core of the membrane. The subunit H of the reaction center is linked with DSP at a low concentration, either with itself or with other membrane proteins but not to the subunits M and L. In isolated reaction centers the subunits H are exclusively linked with each other. With increasing concentrations of DSP the bands of the subunits M, L, and the light-harvesting polypeptide disappear simultaneously from the gel, suggesting that these proteins are linked together. This hypothesis is supported by the finding that reaction centers isolated from chromatophores treated with DSP retain an appreciable amount of light-harvesting polypeptide. With increasing concentrations of the hydrophilic cross-linking reagent glutaraldehyde, the bands of all the three subunits of the reaction center, H, M, and L, progressively disappear from the gel, suggesting that they are linked together. The light-harvesting polypeptide remains free when this reagent is used.

Aldehydes↗

PubMed1983

Redox potential dependence of photophosphorylation and electron transfer in continuous illumination of Rhodopseudomonas sphaeroides chromatophores.

The dependence on redox potential (Eh) of the steady-state photophosphorylation rate in chromatophores of Rhodopseudomonas sphaeroides Ga was measured using slowly equilibrating (and hence less interfering) redox mediators. The remaining interference of the mediators was taken into account by extrapolating to zero mediator concentration. The extents of cytochrome redox reactions (in the presence of antimycin) and of the carotenoid shift were similarly measured. The redox titration of cytochrome c oxidation is consistent with a requirement for prior cytochrome c2 reduction and prior Q1 (primary electron acceptor) oxidation, while the titration of cytochrome b reduction is consistent with a requirement for prior (BChl)2 reduction and prior cytochrome b560 oxidation. The steady-state carotenoid shift extent is a much more broadly peaked function of Eh than is the extent following a single-turnover flash, indicating that the transmembrane electrical potential difference can be built up to significant levels by minimal rates of electron flow. The photophosphorylation rate, in contrast, is much more strongly Eh dependent, supporting the concept of a threshold membrane energization below which phosphorylation cannot occur. Earlier work by others showing a requirement for equilibrium cytochrome c2 reduction and Q1 oxidation is clearly confirmed. A much greater enhancement in phosphorylation rate was found at low Eh than has heretofore been reported. This threefold enhancement is discussed in relation to the equilibrium redox states of the ubiquinone-10 complement of the chromatophore membrane.

Bacterial Chromatophores↗

PubMed1985

Calibration of the response of 9-amino acridine fluorescence to transmembrane pH differences in bacterial chromatophores.

The spectral characteristics of absorption and fluorescence emission of 9-amino acridine are not altered by the interaction with bacterial chromatophores, except for the attenuation of both the absorption and emission following the formation of a protonic gradient. The lifetime of fluorescence of the dye is significantly affected in the presence of membranes, and even more following illumination. The shortening of the lifetime induced by light is reversible and prevented by nigericin and K+. The onset kinetics of the fluorescence quenching following the generation of an artificial transmembrane pH difference is temperature dependent, with an activation energy of 17 +/- 3 kcal/mol. The effect of pH on the rate constants is consistent with a model assuming that the diffusion of the unprotonated species is the limiting step in the quenching phenomenon. The response of 9-amino acridine to artificially imposed delta pH's has been utilized as a calibration method for the measurements of the light-induced protonic gradient. The apparent inner volume of chromatophores, evaluated from the extraplation of the response at delta pH = 0, was found to be much larger (15- to 40-fold) than the true osmotic volume, indicating that most of the dye is bound to the membrane when accumulated into the inner lumen.

Aminacrine↗

PubMed1989

delta pH driven energy-linked NAD+ reduction in Rhodospirillum rubrum chromatophores.

An artificial proton gradient provided sufficient energy to drive reverse electron transport from succinate to NADH:ubiquinone oxidoreductase in chromatophores isolated from Rhodospirillum rubrum. The pH gradient created was able to reduce NAD+. In chromatophores, the optimal rate of NAD+ reduction was about 0.4-0.45 mumol NADH formed/min.mumol bacteriochlorophyll at delta pH 3. The presence of oligomycin was an obligate factor in the assay in order to observe the maximal rate of NAD+ reduction. The rate of NADH formation was dependent on the size of the induced pH gradient. The total NADH formed had a threshold value for the imposed delta pH. The effect of different inhibitors and uncouplers was demonstrated. Comparison between ATP, PPi, and light with the pH jump driven NAD+ reduction rate was studied.

Adenosine Triphosphate↗

PubMed1975

Localization of photosynthetic reaction centers by antibody binding to chromatophore membranes from Rhodopseudomonas spheroides strain R26.

Rabbit antiserum against highly purified reaction center preparations was shown to react specifically with a single component of chromatophore membranes from Rhodopseudomonas spheroides strain R-26. The conjugate of purified gamma globulin and ferritin prepared with toluene diisocyanate was used to determine the localization of reaction centers in the chromatophore membranes. Virtually no antibody was bound by intact membranes. After removing the 9nm ATPase from these membranes by dilute EDTA treatment, a considerable amount of antibody was bound to the exposed outer membrane surface. The reaction center binding sites were estimated to be uniformly distributed with approx. 1 reaction center per 200 nm-2 of membrane surface. These results indicate that the reaction centers are located near the outer membrane surface but below the ATPase particles. Since the distribution of reaction centers and particles on rough faces seen by freeze-fracture particle may be a complex of a reaction center and other electron transfer components localized within the hydrophobic region of the membrane.

Animals↗

PubMed1975

Nature of photochemical reactions in chromatophores of Chromatium D. III. Heterogeneity of the photosynthetic units.

The effect of isooctane extraction on photooxidation of c-type cytochromes was investigated in Chromatium chromatophores. Photooxidation of cytochrome c-555 was not affected by isooctane-extraction was abolished by thorough extraction of ubiquinone-7, but the quantum yield of the cytochrome photooxidation remained unchanged until 90% of the total ubiquinone was extracted. The photooxidation of cytochrome c-552 was recovered by the addition of ubiquinone-7 but not by menaquinone. A dark incubation of sufficient length was needed for maximal quantum yield of cytochrome c-555 photooxidation in the presence of 30 mM ascorbate. It is proposed that there are two types of photosynthetic units (or associations of molecules involved in the primary redox reactions) in Chromatium chromatophores. The combinations of primary electron donor-reaction center chlorophyll-primary electron acceptor may be cytochrome c-552-P890=ubiquinone in one type and cytochrome c-555-P890-X in another.

Ascorbic Acid↗

PubMed1979

Correlation between ATP synthesis and the decay of the arotenoid band shift after single flash activation of chromatophores from Rhodopseudomonas capsulata.

ATP synthesis and the acceleration of the decay of the carotenoid absorption band shift after single flash excitation of Rhodopseudomonas capsulata chromatophores were compared. The two processes behave similarly with respect to: (1) ADP and Pi concentration; (2) inhibition by efrapeptin and venturicidin, and (3) inhibition by valinomycin/K+ and by ionophores. Taken together with earlier evidence for the electrochromic nature of the carotenoid band shift the data support the contention that positive charge moves outwards across the chromatophore membrane during ATP synthesis and justify the method for determination of the H+/ATP ratio (Petty, K.M. and Jackson, J.B. (1979) FEBS Lett. 97, 367-372). The ability of nucleotide diphosphates in the presence of Pi and Mg2+ to give rise to the acceleration of the carotenoid shift decay closely correlates with the rate of phosphorylation of the nucleotides in steady-state light. Nucleotide triphosphates enhance the decay in parallel with their rate of hydrolysis. Adenylyl imidodiphosphate is itself without effect on the decay of the carotenoid shift and it does not prevent the ADP-induced acceleration. The analogue does prevent the ATP effect but only after repeated flashes.

Adenosine Triphosphatases↗

PubMed1979

Kinetic factors limiting the synthesis of ATP by chromatophores exposed to short flash excitation.

ATP synthesis was measured after chromatophores from Rhodopseudomonas capsulata had been subjected to illumination by single turnover flashes fired at variable frequencies. Three processes were examined, which under different conditions can limit the net yield of ATP. (1) A process with an apparent relaxation time of 10-20 ms. This reaction probably limits the rate of ATP synthesis in continuous illumination. It has similar time dependence to the stimulation of the carotenoid shift decay by ADP after a single flash. (2) An active state of the ATPase only persists when the chromatophores are excited more often than once in 10 s. This state decays with similar kinetics to the entire carotenoid shift decay. Full activation is achieved after two flashes. (1) and (2) are not significantly affected by concentrations of antimycin A sufficient to block electron flow through the cytochrome b/c2 oxidoreductase and abolish phase III in the generation of the carotenoid shift. (3) In the presence of antimycin A, after the third, fourth and subsequent flashes ATP synthesis is limited by the quantity of reducing equivalents transported through the reaction centre rather than by the level of the electrochemical proton gradient.

Adenosine Triphosphate↗

PubMed1979

The orientations of reaction center transition moments in the chromatophore membrane of Rhodopseudomonas sphareroides, bases on new linear dichroism and photoselection measurements.

Chromatophore membranes from Rhodopseudomonas sphaeroides were oriented by drying suspensions on the surfaces of glass slides, Polarized spectra of light-induced absorption changes were obtained between 500 and 1000 nm. As observed earlier, these spectra showed negative bands, reflecting photooxidation of the bacteriochlorophyll 'special pair' in the reaction centers, centered near 870, 810, 630 and 600 nm. These bands have been designated BY1, BY2, BX1 and BX2, respectively, corresponding to two QY transitions and two QX transitions of the dimeric special pair. We found the BY1 and BX1 transition moments to be parallel (within 20 degrees) to the plane of the membrane, whereas the BX2 moment makes an angle of 55--63 degrees with the plane. Using the photoselection technique we found that the angle between the BY1 and BX1 transition moments is 30 degrees, while that between BY1 and BX2 is 75 degrees. The BX1 and BX2 moments were found to be orthogonal, consistent with the prediction of molecular exciton theory for a dimer. By combining these data, we have calculated the orientations of the transition moments of the bacteriochlorophyll dimer in spherical polar coordinates, with the pole of the coordinate system normal to the plane of the membrane. The orientations of the QY and QX transition moments of the two bacteriopheophytin molecules in the reaction center were also computed in this coordinate system by transforming the data reported by Clayton, C.N., Rafferty, R.K. and Vermeglio, A. ((1979) Biochim. Biophys. Acta 545, 58--68). We have derived the transformation equations for two polar coordinate systems: in one, the pole is an axis of symmetry as defined by the orientations of purified reaction centers in stretched gelatin films (Rafferty, C.N. and Clayton, R.K. (1979) Biochim. Biophys. Acta 545, 106--121). In the other, the pole is normal to the plane of the chromatophore membrane. These two polar axes are approximately orthogonal.

Bacterial Chromatophores↗