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At least 271 records · Page 15Linked to original sources

PubMed1993

Chromatophoromas and chromatophore hyperplasia in Pacific rockfish (Sebastes spp.).

Pacific rockfish from Cordell Bank, off central California (United States), were collected and histologically examined from 1985 to 1990. Hyperplastic and neoplastic cutaneous lesions, involving dermal chromatophores, were observed in five species; yellowtail rockfish (Sebastes flavidus), bocaccio (S. paucispinis), olive rockfish (S. serranoides), widow rockfish (S. entomelas), and chilipepper rockfish (S. goodei). Yearly prevalences were highest in S. paucispinis (29-38%). Prevalence was initially low in S. flavidus, but increased more than 3-fold from 1985 (7.5%) to 1990 (25%). The majority of lesions were black, but white, yellow, orange, red, and mixed-color variants were also seen. Lesions were found in skin, fins, lips, gingiva, tongue, urogenital papilla, conjunctiva, and cornea of the eye. Flat lesions were consistent with melanophore (black), xanthophore (yellow or orange), and erythrophore (red) hyperplasia. Neoplastic lesions included melanophoromas, amelanotic melanophoromas, xanthophoromas, erythrophoromas, and mixed chromatophoromas. Although etiology has not been determined, interest is currently focused on potential exposure to chemical and radioactive carcinogens from the Farallon Island Radioactive Waste Dump, 30 km to the south.

Animals↗

PubMed1989

The effect of equisetin on energy-linked reactions in Rhodospirillum rubrum chromatophores.

Light-induced proton uptake, light-induced carotenoid absorbance shift, photophosphorylation, and hydrolysis of Mg-ATP, Ca-ATP, and PPi in Rhodospirillum rubrum chromatophores are shown to be inhibited by the antibiotic equisetin. The Mg- and Ca-ATPase activities of purified F0F1-ATPase are inhibited by equisetin. In contrast, only the Ca-ATPase activity of purified F1-ATPase is decreased by equisetin, whereas the Mg-ATPase is stimulated. Both equisetin and N,N'-dicyclohexylcarbodiimide (DCCD) inhibit the hydrolytic activity of the purified H+-PPase but not the hydrolytic activity of soluble PPase from R. rubrum and yeast. The I50 for the PPi hydrolysis is near 20 microM for both equisetin and DCCD. The action of equisetin on membranes is compared to the effect of Triton X-100 and carbonyl cyanide p-trifluoromethoxyhydrazone. On the basis of these new data, equisetin is proposed to act nonspecifically on membranes and hydrophobic domains of proteins.

Adenosine Triphosphate↗

PubMed1990

A rapid burst preceding the steady-state rate of H(+)-transhydrogenase during illumination of chromatophores of Rhodobacter capsulatus. Implications for the mechanism of interaction between protonmotive force and enzyme.

At the onset of illumination of chromatophores there was a burst (t1/2 approx. 5 ms) in the rate of the H(+)-transhydrogenase reaction before establishment of the steady-state rate. The burst was suppressed at high pH with a pKa of approx. 8.5. The burst and the steady-state rate were inhibited by either (i) a combination of myxothiazol and carbonylcyanide-p-trifluoromethoxyphenylhydrazone, or (ii) NAD+, or (iii) dicyclohexylcarbodiimide. The results support a model in which substrate binding to H(+)-transhydrogenase is relatively fast. A subsequent slow step is accelerated by the protonmotive force and a third step, possibly product release, is rate-limiting in steady-state turnover during illumination.

Hydrogen-Ion Concentration↗

PubMed1990

Partial reversion of the electrogenic reaction in the ubiquinol: cytochrome c2-oxidoreductase of Rhodobacter sphaeroides chromatophores under neutral and alkaline conditions.

The interaction of the photosynthetic reaction center (RC)-generated ubiquinol with the ubiquinone-reducing center C of ubiquinol:cytochrome c2-oxidoreductase (bc1-complex) has been studied electrometrically in Rhodobacter sphaeroides chromatophores. The addition of myxothiazol inhibited the ubiquinol-oxidizing center Z, suppressing the phases of membrane potential generation by the bc1-complex, but at the same time induced an electrogenic phase of opposite polarity, sensitive to antimycin A, the inhibitor of center C. The rise time of this reverse phase varied from 3 ms at pH 6.0 to 1 ms at pH 9.5. At pH greater than 9.5 the reverse phase was limited by the rate of ubiquinol formation in RC. The magnitude of the reverse phase was constant within the pH range 7.5-10.0. It is assumed that the reverse phase is due to the electrogenic deprotonation reaction which takes place after the binding of the RC-generated ubiquinol to center C.

Cytochrome c Group↗

PubMed1991

Antibiotic production by the marine photosynthetic bacterium Chromatium purpuratum NKPB 031704: localization of activity to the chromatophores.

Over 200 strains of marine purple photosynthetic bacteria were isolated. Two strains showed antibiotic activity towards Saccharomyces cerevisiae and were tentatively identified as Chromatium purpuratum. Crude antibiotic, prepared by solvent extraction, showed a broad antimicrobial spectrum. The highest activity was found in the chromatophore fraction. Chromatographic separation of purified light harvesting complex from one strain, NKPB 031704, showed the presence of two separate pigmented compounds which were responsible for antimicrobial activity. Our findings reveal the unexpected ability of photosynthetic bacteria to produce broad spectrum antibiotics. In addition, this is the first example of intracellular localization of antibiotic activity in a marine bacterium.

Anti-Bacterial Agents↗

PubMed2001

Equilibrium and kinetic parameters for the binding of inhibitors to the QB pocket in bacterial chromatophores: dependence on the state of QA.

The equilibrium and kinetic parameters for the binding of various inhibitors to the Q(B) pocket of the bacterial reaction center were investigated in chromatophores from Rhodobacter capsulatus and Rhodobacter sphaeroides. By monitoring the near-IR absorption changes specific to Q(A)(-) and Q(B)(-), we measured the fraction of inhibited centers in the dark and the kinetics and extent of inhibitor displacement after one flash due to the formation of the Q(A)Q(B)(-) state. The inhibitor release rate was much faster for triazines and o-phenanthroline (t(1/2) in the 50 ms to 1 s range) than for stigmatellin (t(1/2) approximately 20 s). For inhibitors with a rapid release rate, the fast phase of P(+) decay observed in the absence of secondary donor reflects the competition between P(+)Q(A)(-) recombination and inhibitor release: it is thus faster than the P(+)Q(A)(-) recombination, and its relative extent is smaller than the fraction of initially inhibited centers. At appropriate inhibitor concentrations, one can have almost total binding in the dark and almost total inhibitor displacement after one flash. Under such conditions, a pair of closely spaced flashes resets the two-electron gate in a single state (Q(A)Q(B)(-)), irrespective of the initial state. The apparent dissociation constant of terbutryn was significantly increased (by a factor of 4-7) in the presence of Q(A)(-), in agreement with the conclusion of Wraight and co-workers [Stein, R. R., et al. (1984) J. Cell. Biochem. 24, 243-259]. We suggest that this effect is essentially due to a tighter binding of ubiquinone in the Q(A)(-) state.

Anti-Bacterial Agents↗

PubMed1979

Photooxidation of antenna bacteriochlorophyll in chromatophores from carotenoidless mutant Rhodopseudomonas sphaeroides and the attendant loss of dimeric exciton interaction.

Intense continuous illumination of purified chromatophores from carotenoidless mutant Rhodopseudomonas sphaeroides results in progressive photooxidative loss of the near infrared absorption band near 860 nm assigned to antenna bacteriochlorophyll. The quantum yield of this reaction is low, approximately 1.7 x 10(-5). The loss in near infrared absorption is accompanied by a proportional shift in the absorption maximum to shorter wavelengths. The double circular dichroism feature in the near infrared decreases at a faster rate than does the absorbance. These results are explained by a model in which the antenna bacteriochlorophyll, initially associated as dimers (lambda(max) = 860.2 nm), is progressively converted to the monomeric state (lambda(max) = 851.9 nm). The wavelength shift is attributed to disruption of exciton coupling in the dimer. Acetone/methanol extraction indicates that the maximum molar extinction coefficients of the dimer and monomer do not differ by more than 4%. The occurrence of an absorption maximum at 852 nm for monomeric bacteriochlorophyll in a protein complex demonstrates that it is not necessary to invoke aggregation of the chromophores as the origin of the shift from 770 nm in typical organic solvents.

Journal Article↗

PubMed1984

Tunneling in Chromatium chromatophores: Detection of a Hopfield charge-transfer band.

We have observed a weak charge-transfer band in the cytochrome c-P(870) electron-transfer reaction in Chromatium vinosum chromatophores at 10 K and at 85 K. First, the intermediate acceptor, I, was trapped in the reduced state by lowering the redox potential at room temperature, then illuminating with white light at low temperature for 20 min. Next, illumination by broadband infrared (1-3 mum, 6.5 kW/m(2)) for 4 hr at 10 K decreased the I(-) electron spin resonance signal by 30%. One-hour infrared illumination at 85 K decreased the cytochrome c Soret band shift by 10%. The effect of infrared was to promote the system from the ground vibrational state with the electron on P(870) to an excited vibrational state with the electron on cytochrome c. The absorption band peak is near 2 mum, and the integrated cross section is approximately 6 x 10(-3) eV.M(-1).cm(-1). These values are consistent with small (0.02 nm) nuclear motion and with electron-transfer rates measured in the dark.

Journal Article↗

PubMed1972

Biocarbonate Effect on the Photophosphorylation Catalyzed by Chromatophores Isolated from Chromatium Strain D: XII. Structure and Function of Chloroplast Proteins.

Photophosphorylation catalyzed by chromatophores prepared from Chromatium strain D was stimulated by bicarbonate. The stimulative effect was pH dependent and the lower the pH the more marked the activation. At pH 8.0, bicarbonate (8 mm) exhibited a negligible effect, whereas at pH 7.0 approximately a 5-fold activation was observed. The apparent activation constant of bicarbonate was determined to be approximately 10.2 mm, at which concentration approximately a 7-fold activation of photophosphorylation was observed.

Journal Article↗

PubMed1997

Dinitrogenase reductase-activating glycohydrolase can be released from chromatophores of Rhodospirillum rubrum by treatment with MgGDP.

Dinitrogenase reductase-activating glycohydrolase (DRAG), involved in the regulation of nitrogenase activity in Rhodospirillum rubrum, is associated with chromatophore membranes in cell extracts. We show that DRAG can be specifically released by treatment with MgGDP; other nucleotides studied had no effect. The DRAG activity released corresponds to the release of DRAG protein.

Enzyme Activation↗

PubMedDate not supplied

[Features of transformation of phosphates in Rhodobacter sphaeroides chromatophores].

We have found the ATP production in the Rhodobacter sphaeroides chromatophores illuminated by single short light flash, that is under conditions when the proton gradient formed as a result of electron transport after the second flash, is absent. The ATP synthesis was accompanied by the H2O2 formation. Simultaneous formation of H2O2 is indicative of the oxidative activation of phosphate during the ATP synthesis, as in the model systems with isolated chlorophyll. These data provide a theoretical background to the fitting of illumination parameters in both laboratory and industrial photobioreactors with photosynthetic bacteria used in biotechnological processes.

Adenosine Triphosphate↗

PubMed1977

[Photoreduction of bacteriophenophytin b in the primary light reaction of Rhodopseudomonas viridis chromatophores].

Photoconversions of the reaction center pigments in chromatophores of nonsulfur purple bacteria Rhodopseudomonas viridis have been studied as a function of redox potential of medium (Eh). It has been shown that at a decrease in the Eh values from +400 mV to--100 divided by--600 mV a photo-induced accumulation of P980+ (oxidized primary electron donor in R. viridis) is replaced by the photoaccumulation of a reduced pigment complex P800 (bleaching of bacteriopheophytin b absorption bands at 545 and 800 nm, a development of broad bands at 680 and 430 nm and a blue shift of the bacteriochlorophyll band at 830 nm). The P800 photoreduction is observed under illumination by light with lambda greater than 900 nm between +20 divided by--196 degrees C at pH 3,5--12,5 and is accompanied by oxidation of the cytochrome and an increase in fluorescence yield of bacteriochlorophyll. It is suggested that P800 accepts an electron from the P980 in the primary photoreaction, which preceeds ubiquinone reduction. A midpoint redox potential (Em) is found to be of --620(+/- 20) mV for the P800/P800- and +515 (+/-20) mV for the P980/+P980. At a decrease in the Eh value down to -400 mV luminescence has been detected with T1/2 8 nsec, an activation energy of 0,065 +/- 0,02 ev and quantum yield being close to the fluorescence yield. It is assumed that this luminescence is a result of charge recombination in the biradical P980+ -- P800-.

Chlorophyll↗

PubMed1963