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PubMed1978

Properties of photochemical reaction centers purified from Rhodopseudomonas gelatinosa.

Reaction centers were isolated from a carotenoidless mutant of Rhodopseudomonas gelatinosa by hydroxyapatite chromatography of purified chromatophores treated with lauryl dimethyl amine oxide. Absorption spectra and spectra of light-induced absorbance changes are similar to those of reaction centers from Rhodopseudomonas sphaeroides. The ratio of absorbance at 280 nm to that at 799 nm was 1.8 in the purest preparations. The extinction coefficient at the 799 nm absorption maximum was estimated to be 305 +/- 20 mM--1 . CM--1. The molecular weight based on protein and chromophore assays was found to be 1.5 . 10(5); the reaction center protein accounted for 6% of the total membrane protein. These reaction centers contained no cytochrome and showed just two components of apparent molecular weights 33 000 and 25 000 in polyacrylamide gel electrophoresis. The chromatophores contained 42 molecules of antenna bacteriochlorophyll for each reaction center.

Bacterial Chromatophores↗

PubMed1978

The mechanism of reduction of the ubiquinone pool in photosynthetic bacteria at different redox potentials.

(1) A flash number dependency of flash-induced absorbance changes was observed with whole cells of Rhodospirillum rubrum and chromatophores of R. rubrum and Rhodopseudomonas sphaeroides wild type and the G1C mutant. The oscillatory behavior was dependent on the redox potential; it was observed under oxidizing conditions only. Absorbance difference spectra measured after each flash in the 275--500 nm wavelength region showed that a molecule of ubiquinone, R, is reduced to the semiquinone (R-) after odd-numbered flashes and reoxidized after even-numbered flashes. The amount of R reduced was approximately one molecule per reaction center. (2) The flash number dependency of the electrochromic shift of the carotenoid spectrum was studied with chromatophores of Rps. sphaeroides wild type and the G1C mutant. At higher values of the ambient redox potential a relatively slow phase with a rise time of 30 ms was observed after even-numbered flashes, in addition to the fast phase (completed within 0.2 ms) occurring after each flash. Evidence was obtained that the slow phase represents the formation of an additional membrane potential during a dark reaction that occurs after flashes with an even number. This reaction is inhibited by antimycin A, whereas the oscillations of the R/R- absorbance changes remain unaffected. At low potentials (E = 100 mV) no oscillations of the carotenoid shift were observed: a fast phase was followed by a slow phase (antimycin-sensitive) with a half-time of 3 ms after each flash. (3) The results are discussed in terms of a model for the cyclic electron flow as described by Prince and Dutton (Prince, R.C. and Dutton, P.L. (1976) Bacterial Photosynthesis Conference, Brussels, Belgium, September 6--9, Abstr. TB4) employing the so-called Q-cycle.

Bacterial Chromatophores↗

PubMed1979

Oxonol dyes as monitors of membrane potential. Their behavior in photosynthetic bacteria.

The reponses of oxonol dyes to single and multiple single turnovers of the photosynthetic apparatus of photosynthetic bacteria have been studied, and compared with the responses of the endogenous carotenoid pigments. The absorbance changes of the oxonols can be conveniently measured at 587 nm, because this is an isosbestic point in the 'light-minus-dark' difference spectrum of the chromatophores. The oxonols appear to respond to the light-induced 'energization' by shifting their absorption maxima. In the presence of K+, valinomycin abolished and nigericin enhanced such shifts, suggesting that the dyes, respond to the light-induced membrane potential. Since the dyes are anions at neutral pH values, they probably distribute across the membrane in accordance with the potential, which is positive inside the chromatophores. The accumulation of dye, which is indicated by a decrease in the carotenoid bandshift, poises the dye-membrane equilibrium in favor of increased dye binding and this might be the cause of the spectral shift. The dye response has an apparent second-order rate constant of approx. 2 . 10(6) M-1 . s-1 and so is always slower than the carotenoid bandshift. Thus the dyes cannot be used to monitor membrane potential on submillisecond timescales. Nevertheless, on a timescale of seconds the logarithm of the absorbance change at 587 nm is linear with respect to the membrane potential calibrated with the carotenoid bandshift. This suggests that under appropriate conditions the dyes can be used with confidence as indicators of membrane potential in energy-transducing membranes that do not possess intrinsic probes of potential.

Antimycin A↗

PubMed1979

Membranes of Rhodopseudomonas sphaeroides. VII. Photochemical properties of a fraction enriched in newly synthesized bacteriochlorophyll a-protein complexes.

Previous pulse-chase studies have shown that bacteriochlorophyll a-protein complexes destined eventually for the photosynthetic (chromatophore) membrane of Rhodopseudomonas sphaeroides appear first in a distinct pigmented fraction. This rapidly labeled material forms an upper band when extracts of phototrophically grown cells are subjected directly to rate-zone sedimentation. In the present investigation, flash-induced absorbance changes at 605 nm have demonstrated that the upper fraction is enriched two-fold in photochemical reaction center activity when compared to chromotophores; a similar enrichment in the reaction center-associated B-875 antenna bacteriochlorophyll complex was also observed. Although b- and c-type cytochromes were present in the upper pigmented band, no photoreduction of the b-type components could be demonstrated. The endogenous c-type cytochrome (Em = +345 mV) was photooxidized slowly upon flash illumination. The extent of the reaction was increased markedly with excess exogenous ferrocytochrome c but only slightly in chromatophores. Only a small light-induced carotenoid band shift was observed. These results indicate that the rapidly labeled fraction contains photochemically competent reaction centers associated loosely with c-type and unconnected to b-type cytochrome. It is suggested that this fraction arises from new sites of cytoplasmic membrane invagination which fragment to form leaky vesicles upon cell disruption.

Bacterial Chromatophores↗

PubMed1984

Cell-cycle-specific biosynthesis of the photosynthetic membrane of Rhodopseudomonas sphaeroides. Structural implications.

Structural changes association with the intracytoplasmic membrane during the cell cycle of the photosynthetic bacterium Rhodopseudomonas sphaeroides have been studied by freeze-fracture electron microscopy. The isolated intracytoplasmic membrane vesicles, chromatophores, were fused in order to obtain large fracture faces, allowing more precise measurements and statistical analysis of both intramembrane particle density and size determinations. The intramembrane particle density of the protoplasmic face (PF) of the intracytoplasmic membrane, (from 4970 to 8290/micrometers 2), was shown to be a linear function of the protein/phospholipid ratio (from 2.5 to 5.1, w/w) of the intracytoplasmic membrane. Under constant light intensity, both the average particle size and particle size distribution remained unchanged during the cell cycle. These results provide the structural basis for the earlier reported cell-cycle-specific variations in both protein/phospholipid ratio and alternation in phospholipid structure of the intracytoplasmic membrane of R. sphaeroides during photosynthetic growth. The average particle diameter in the PF face of the intracytoplasmic membrane was 8.25, 9.08 and 9.75 nm at incident light intensities of 4000, 500 and 30 ft X cd, respectively. When chromatophores were fused with small, unilamellar liposomes, the intramembrane particle density decreased as input liposome phospholipid increased, whereas the particle size remained constant and particle distribution became random.

Bacterial Chromatophores↗

PubMed1983

The existence of an antimycin A insensitive ubiquinol-cytochrome c reductase activity in the photosynthetic apparatus.

A nonproteinaceous, antimycin A insensitive ubiquinol-cytochrome c reductase activity is detected in and purified from chromatophores of Rhodopseudomonas sphaeroides, R-26. This activity is about 5 times the antimycin A sensitive reductase activity in chromatophores and the two are not interconvertable. The purification involved chloroform:methanol (2:1), and hexane extractions and florisil column chromatography. The purified preparation contains some bacteriochlorophyll-like pigments and phospholipids, and is stable in organic solvent. It catalyzes the oxidation of ubiquinol by cytochrome c with substrate specificity and pH optimum.

Antimycin A↗

PubMed1993

Differential sensitivity of membrane-associated pyrophosphatases to inhibition by diphosphonates and fluoride delineates two classes of enzyme.

1,1-Diphosphonate analogs of pyrophosphate, containing an amino or a hydroxyl group on the bridge carbon atom, are potent inhibitors of the H(+)-translocating pyrophosphatases of chromatophores prepared from the bacterium Rhodospirillum rubrum and vacuolar membrane vesicles prepared from the plant Vigna radiata. The inhibition constant for aminomethylenediphosphonate, which binds competitively with respect to substrate, is below 2 microM. Rat liver mitochondrial pyrophosphatase is two orders of magnitude less sensitive to this compound but extremely sensitive to imidodiphosphate. By contrast, fluoride is highly effective only against the mitochondrial pyrophosphatase. It is concluded that the mitochondrial pyrophosphatase and the H(+)-pyrophosphatases of chromatophores and vacuolar membranes belong to two different classes of enzyme.

Animals↗

PubMed1981

Hyperpigmented patches in the skin of the newt Notophthalmus viridescens.

In the integument of the red-spotted newt there occasionally appear patches of skin which are at the same time melanistic and iridescent. Such hyperpigmented patches have been found on the back, on the tail and on the dorsal surface of both fore and hind limbs. Cytological examination of several such areas revealed the presence of large numbers of chromatophores distributed throughout the dermis. The majority of the chromatophores consisted of atypically large and dendritic melanophores, which contained typical pigment granules. The iridescence resulted from a high incidence of iridophores. Xanthophores also were found in considerable abundance. This extensive and apparently random intermingling of melanophores, iridophores and xanthophores in limited areas constitutes a striking exception to the usual distributional patterns of pigment cells in this animal.

Animals↗

PubMed1979

Scotophobin A causes several responses in goldfish if the pineal gland is present.

Rat scotophobin A increased dark avoidance in goldfish in dark and light avoidance shuttlebox experiments, controlled for general and light cycling-induced swimming activity. A possible site of action for scotophobin was suggested by the reports that dark avoidance was also increased in goldfish by pinealectomy, a treatment which increased shock sensitivity as well. It was found that scotophobin alone decreased the voltage required to induce tail-flip contractures in goldfish. The pineal gland was further implicated in the mode of action of scotophobin when it was found that this peptide suppressed the norepinephrine-induced aggregation of goldfish chromatophores whose state is in part controlled by pineal melatonin. Pinealectomized goldfish became insensitive to the effects of scotophobin upon both light-dark preference and chromatophore aggregation state. There observations strongly suggest that the pineal gland is required for the action of scotophobin.

Animals↗

PubMed1986

Opioid potentiated chromatophorotropin regulation of pigment migration in the land crab Gecarcinus lateralis.

In Gecarcinus lateralis dopamine treatment results in dispersion of black and concentration of red pigments within chromatophores. These effects of dopamine on the migration of pigments can be blocked by the dopamine antagonist haloperidol. These results strongly indicate the presence of a dopamine receptor mediated system in this organism. Serotonin injections also result in the dispersion of black pigment; however, this effect cannot be blocked by haloperidol. Norepinephrine was found to be without effect on this pigment regulatory system. Injections of crude eyestalk extract results in pigment migration within the chromatophores in both stalked and destalked animals. Injection of the stable methionine enkephalin analog FK 33 824 into the organisms causes no observable effects on the pigment system. However, coinjection with eyestalk extract strongly potentiates the effect of the extract. This potentiation can be completely blocked by the opiate antagonist naloxone, thus indicating that an endogenous opioid system may be part of the overall regulation of pigmentation movement.

Animals↗

PubMed2005

Spectral analysis of the bc(1) complex components in situ: beyond the traditional difference approach.

The cytochrome (cyt) bc(1) complex (ubiquinol: cytochrome c oxidoreductase) is the central enzyme of mitochondrial and bacterial electron-transport chains. It is rich in prosthetic groups, many of which have significant but overlapping absorption bands in the visible spectrum. The kinetics of the cytochrome components of the bc(1) complex are traditionally followed by using the difference of absorbance changes at two or more different wavelengths. This difference-wavelength (DW) approach has been used extensively in the development and testing of the Q-cycle mechanism of the bc(1) complex in Rhodobacter sphaeroides chromatophores. However, the DW approach does not fully compensate for spectral interference from other components, which can significantly distort both amplitudes and kinetics. Mechanistic elaboration of cyt bc(1) turnover requires an approach that overcomes this limitation. Here, we compare the traditional DW approach to a least squares (LS) analysis of electron transport, based on newly determined difference spectra of all individual components of cyclic electron transport in chromatophores. Multiple sets of kinetic traces, measured at different wavelengths in the absence and presence of specific inhibitors, were analyzed by both LS and DW approaches. Comparison of the two methods showed that the DW approach did not adequately correct for the spectral overlap among the components, and was generally unreliable when amplitude changes for a component of interest were small. In particular, it was unable to correct for extraneous contributions to the amplitudes and kinetics of cyt b(L). From LS analysis of the chromophoric components (RC, c(tot), b(H) and b(L)), we show that while the Q-cycle model remains firmly grounded, quantitative reevaluation of rates, amplitudes, delays, etc., of individual components is necessary. We conclude that further exploration of mechanisms of the bc(1) complex, will require LS deconvolution for reliable measurement of the kinetics of individual components of the complex in situ.

Bacterial Chromatophores↗

PubMed2006

Constructing a novel Nanodevice powered by delta-free FoF1-ATPase.

A Nanodevice was constructed by delta-free F(o)F(1)-ATPase within chromatophores and actin filaments through biotinlipid-streptavidin-biotin-(AC(5))(2)Sulfo-OSu system. One actin filament linking with many chromatophores functions as the Nanodevice body and many delta-free F(o)F(1)-ATPase as the Nanodevice motors. Movement of the Nanodevice was observed directly by fluorescence microscopy with CCD camera after illumination. The moving speed was about 2.17-24.43mum/s for various length Nanodevices and most of them were stopped by adding CCCP. This means that the Nanodevice was driven by PMF (proton-motive force) in the cooperating delta-free F(o)F(1)-ATPase. From bioengineering point of view, the cooperation of F(o)F(1)-ATPase is a very important research field in the future.

Actins↗

PubMed2005

A low-cost, portable generic biotoxicity assay for environmental monitoring applications.

Fish chromatophores have been shown to be promising biosensors for the detection of hostile agents in the environment. However, state-of-art methods for such applications are still based on extensive use of data/signal processing, in conjunction with need for a skilled human observer to carry out the detection. As a result, conventional methods are complex, costly and cumbersome rendering them useless for field applications requiring low-cost portable solutions capable of fast detection. A new technique is proposed based on the popular scheme of observing the aggregation response in chromatophores for detection of toxicity, and a solution using optical detection and electronic processing is outlined. This scheme has the advantage of being low in cost while providing simple, fast and reliable detection.

Animals↗

PubMed1997

The pH dependences of reactions catalyzed by the complete proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains.

Transhydrogenase couples the translocation of protons across a membrane to the transfer of reducing equivalents between NAD(H) and NADP(H). Using transhydrogenase from Rhodospirillum rubrum we have examined the pH dependences of the 'forward' and 'reverse' reactions, and of the 'cyclic' reaction (NADP(H)-dependent reduction of the analogue, acetyl pyridine adenine dinucleotide, by NADH). In the case of the membrane-bound protein in chromatophores, the imposition of a protonmotive force through the action of the light-driven electron-transport system, stimulated forward transhydrogenation, inhibited reverse transhydrogenation, but had no effect on the cyclic reaction. The differential response at a range of pH values provides evidence that hydride transfer per se is not coupled to proton translocation and supports the view that energy transduction occurs at the level of NADP(H) binding. Chromatophore transhydrogenase and the detergent-dispersed enzyme both have bell-shaped pH dependences for forward and reverse transhydrogenation. The cyclic reaction, however, is rapid at low and neutral pH, and is attenuated only at high pH. A mixture of recombinant purified NAD(H)-binding domain I, and NADP(H)-binding domain III, of R. rubrum transhydrogenase carry out the cyclic reaction with a similar pH profile to that of the complete enzyme, but the forward and reverse reactions were much less pH dependent. The rates of release of NADP+ and of NADPH from isolated domain III were pH independent. The results are consistent with a model for transhydrogenation, in which proton binding from one side of the membrane is consequent upon the binding of NADP+ to the enzyme, and then proton release on the other side of the membrane precedes NADPH release.

Bacterial Chromatophores↗

PubMed2002

Behavioral visual responses of wild-type and hypopigmented zebrafish.

Zebrafish possess three classes of chromatophores that include iridophores, melanophores, and xanthophores. Mutations that lack one or two classes of chromatophores have been isolated or genetically constructed. Using a behavioral assay based on visually mediated escape responses, we measured the visual response of fully and partially pigmented zebrafish. In zebrafish that lack iridophores (roy mutants), the behavioral visual responses were similar to those of wild-type animals except at low contrast stimulation. In the absence of melanophores (albino mutants) or both melanophores and iridophores (ruby mutants), the behavioral visual responses were normal under moderate illumination but reduced when tested under dim or bright conditions or under low contrast stimulation. Together, the data suggest that screening pigments in the retina play a role in the regulation of behavioral visual responses and are necessary for avoiding "scatter" under bright light conditions.

Albinism, Ocular↗

PubMed2004

Individual colour patches as multicomponent signals.

Colour patches are complex traits, the components of which may evolve independently through a variety of mechanisms. Although usually treated as simple, two-dimensional characters and classified as either structural or pigmentary, in reality colour patches are complicated, three-dimensional structures that often contain multiple pigment types and structural features. The basic dermal chromatophore unit of fishes, reptiles and amphibians consists of three contiguous cell layers. Xanthophores and erythrophores in the outermost layer contain carotenoid and pteridine pigments that absorb short-wave light; iridophores in the middle layer contain crystalline platelets that reflect light back through the xanthophores; and melanophores in the basal layer contain melanins that absorb light across the spectrum. Changes in any one component of a chromatophore unit can drastically alter the reflectance spectrum produced, and for any given adaptive outcome (e.g. an increase in visibility), there may be multiple biochemical or cellular routes that evolution could take, allowing for divergent responses by different populations or species to similar selection regimes. All of the mechanisms of signal evolution that previously have been applied to single ornaments (including whole colour patches) could potentially be applied to the individual components of colour patches. To reach a complete understanding of colour patch evolution, however, it may be necessary to take an explicitly multi-trait approach. Here, we review multiple trait evolution theory and the basic mechanisms of colour production in fishes, reptiles and amphibians, and use a combination of computer simulations and empirical examples to show how multiple trait evolution theory can be applied to the components of single colour patches. This integrative perspective on animal colouration opens up a host of new questions and hypotheses. We offer specific, testable functional hypotheses for the most common pigmentary (carotenoid, pteridine and melanin) and structural components of vertebrate colour patches.

Animals↗

PubMed1979

Purification of the energy-transducing adenosine triphosphatase complex from Rhodospirillum rubrum.

The oligomycin- and N,N'-dicyclohexylcarbodiimide-sensitive adenosine triphosphatase complex extracted with Triton X-100 from the chromatophores of Rhodospirillum rubrum was extensively purified. The purification procedure included (diethylamino)ethylcellulose chromatography and glycerol gradient centrifugation. The specific activity of Mg2+-dependent ATP hydrolysis in the purified preparation increased about 11-fold, while that of Ca2+-dependent ATP hydrolysis increased 50-fold as compared with chromatophores. The purified adenosine triphosphatase complex dissociated into a maximum of eight different polypeptides upon electrophoresis in the presence of sodium dodecyl sulfate. The estimated subunit molecular weights were as follows: 56 000 (alpha), 50 000 (beta), 33 000 (gamma), and those ranging from 17 000 to 9400 for the remaining smaller subunits. The purified preparation was incorporated into phospholipid vesicles by using the freeze--thaw technique. The reconstituted vesicles catalyzed [32P]ATP exchange, which was almost completely inhibited by both oligomycin and N,N'-dicyclohexylcarbodiimide as well as by a protonophorous uncoupler, carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone.

Adenosine Triphosphatases↗

PubMed1977

Isolation and characterization of an organic solvent soluble polypeptide component from photoreceptor complexes of Rhodospirillum rubrum.

An organic solvent soluble polypeptide has been isolated from photoreceptor complexes and chromatophores of Rhodospirillum rubrum. After extraction of the protein from lyophilized samples with 1:1 chloroform-methanol, it was purified by column chromatography. Its isoelectric point determined by isoelectric focusing was 7.10. When analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified polypeptide ran as a single band of an apparent molecular weight of 12 000. However, according to amino acid analysis, the minimal molecular weight based on one histidine residue per polypeptide is 19 000. The polypeptide contains no cysteine and no tyrosine. Amino acid analysis indicated that three methionines were present per histidine residue and cyanogen bromide cleavage gave four smaller peptides which were isolated by two-dimensional electrophoresis and chromatography. Spectroscopic analysis indicated the presence of three tryptophan residues per histidine and N-bromosuccinamide cleavage also gave four smaller peptides which could be isolated by two-dimensional electrophoresis and chromatography. The C-terminal amino acid was shown to be glycine by two methods, while the N-terminal amino acid appears to be blocked. The organic solvent soluble polypeptide accounts for approximately 50% of the chromatophore protein and seems to bind the antenna bacteriochlorophyll and carotenoid molecules. Using this procedure, organic solvent soluble polypeptides were isolated from several photosynthetic bacteria and were found to have substantially different amino acid contents.

Amino Acids↗