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At least 775 records · Page 43Linked to original sources
PubMed1981

The involvement of a high potential acceptor in the acid-base induced reduction of the acceptor Q in chloroplasts.

Study of the acid-base induced fluorescence transient, the so-called 'reverse electron flow', in chloroplasts revealed the following new properties: (1) Experiments in which the acid-base transition was performed in the absence of the measuring beam showed that the high fluorescence state induced by a pH-jump was attained and decayed even in complete darkness. These results indicated that a non-photochemical electron transfer was affected by the pH transition. A pH-induced reverse electron transfer from some secondary electron acceptor to Q probably occurred during that process. (2) This conclusion was supported by the effect of the Photosystem I electron acceptor methyl viologen. Methyl viologen accelerated the decay phase of the transient showing that this phase was controlled by the rate of electron flow to Photosystem I, but this acceptor did not diminish the size of the transient's initial rise, probably because this rise reflected a pH effect on a non-photochemical step located between Q and P-700. (3) The size of the fluorescence transient was dependent upon the reduction state of both parts of the secondary pool of electron acceptors, A2 and A1. (4) Redox potential measurements using ferricyanide-ferrocyanide mixtures showed that the size of the transient was directly dependent on a midpoint potential of +385 mV at pH 6.9 and with n = 1. This suggested the involvement of a high potential secondary electron acceptor in the acid-base induced reduction of Q.

Chloroplasts↗
PubMed1981

Photosynthetic energy conservation investigated by thermoluminescence. Activation energies and half-lives of thermoluminescence bands of chloroplasts determined by mathematical resolution of glow curves.

Thermoluminescence of isolated chloroplasts was analysed by a computer-assisted multicomponent curve fitting procedure to determine the activation energies, the free energies of activation, frequency factors and half-lives of the component bands of the glow curve. Optimal fit was obtained in the temperature region from -80 degrees C to +80 degrees C by the resolution of the glow curve into seven bands with peak positions at -24, -12, +12, +17, +28, +44, and +69 degrees C. All of the activation free energies of the thermoluminescence bands were much higher than 0.59 eV, the minimum free energy of activation required for the back reaction of the primary charge separation as calculated on the basis of the theory of Ross and Calvin (Ross, R.T. and Calvin, M. (1967) Biophys. J. 7, 595-614). The high free energies of activation and long half-lives (longer than 50 ms) of the thermoluminescence bands suggest that thermoluminescence in the temperature region from -80 degrees C to 80+ C does not reflect the change recombination of primary products but represent the reversal of subsequent stabilization steps of the charge separation process which proceed along the acceptor and donor sides of Photosystem II.

Chloroplasts↗
PubMed1981

Energy transfer from phycobiliproteins to photosystem I in vegetative cells and heterocysts of Anabaena variabilis.

The presence of phycobilins in heterocysts of Anabaena variabilis is established on the basis of absorption and fluorescence spectroscopy. At 77 K heterocysts exhibit fluorescence emission bands at 645 and 661 nm indicative of phycocyanin and allophycocyanin, respectively. Both allophycocyanin levels and fluorescence emission at 695 nm were low in heterocysts relative to whole filaments. In situ fluorescence microscopy confirmed the presence of phycobilins in individual heterocysts, but the pigment levels varied considerably among cells. Heterocysts exhibited Photosystem I activity, as evidenced by photooxidation of P-700, but no Photosystem II activity. The quantum efficiency of phycobilins in sensitizing P-700 photooxidation was 50-70% that of chlorophyll a. Phycoibins were also effective in promoting light-dependent reduction of acetylene to ethylene. The results are discussed in terms of the role of the heterocyst in nitrogen fixation and of the significance of energy transfer from phycobilins to Photosystem I in heterocysts.

Cyanobacteria↗
PubMed1992

Thermoluminescence and flash-induced oxygen yield in herbicide resistant mutants of the D1 protein in Synechococcus PCC7942.

Several strains of Synechococcus PCC7942 carrying point mutations in the gene psbA were studied by thermoluminescence and polarographic measurement of flash-induced oxygen yield. The following results were obtained: (a) Replacement of Ser-264 in D1 by Ala (mutant Di1) or Gly (mutant G264) resulting in DCMU and atrazine resistance leads to a downshift of the thermoluminescence (TL) B-band peak temperature from 40 degrees C in wild-type thylakoids to about 30 degrees C. In dark adapted samples of both mutants the TL and oxygen yield pattern induced by a train of single turnover flashes were strongly damped indicative of a high miss factor. (b) In contrast to Ser-264 mutants, replacement of Phe-255 in D1 by Tyr (mutant Tyr5) induced strong resistance to atrazine but not to DCMU and did not affect the peak termperature of the B-band and the flash-induced TL and oxygen yield patterns. In this respect mutant Tyr5 resembles the wild type. (c) No significant differences have been found between strains with single site mutations in psbAI and normal psbAII/psbAIII genes, and strains with same mutations in psbAI but additional deletion of psbAII and psbAIII. Obviously in strains were psbAI is present, PS II complexes containing gene products of psbAII and psbAIII are not assembled in detectable amounts. (d) Strains with double mutations at positions 264 and 255 display a downshift of the B-band peak temperature. Their oscillatory patterns of B-band intensity and oxygen yield are highly damped. This behaviour is similar to strains D1 and G264 which are modified at position 264 only. We extend reports on additivity of mutation effects on herbicide binding to binding of QB. (e) Mutations at the QB site not only influence the binding of QB and herbicides but also change the thermoluminescence quantum yield and the lifetimes of the redox states S2 and S3 of the water oxidase. This finding might indicate long ranging effects on Photosystem II exerted by structural modifications of the QB site. From these data we conclude that Ser-264 is essential for binding of atrazine, DCMU and QB, whereas Phe-255 is involved in atrazine binding and its substitution by Tyr does not markedly affect QB or DCMU binding in Synechococcus PCC7942.

Atrazine↗
PubMed1993

The mechanisms by which mild respiratory chain inhibitors inhibit hepatic gluconeogenesis.

(1) Liver cells from starved rats were incubated with 10 mM L-lactate, 1 mM pyruvate and 0.3 microM glucagon in the presence and absence of the mild respiratory inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) at 0.5 mM. (2) The whole cell concentrations of phosphoenolpyruvate, 2-phosphoglycerate and 3-phosphoglycerate increased about 2-fold, whilst the triose and hexose phosphate concentrations all decreased significantly. Similar results were obtained with 0.15 microM oligomycin and 10 microM atractyloside. (3) These data can be explained by a substantial decrease in the cytosolic free concentration ratio of ATP/ADP acting on the equilibrium of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase. (4) The increase in cytosolic phosphoenolpyruvate concentration can account for the observed increase in pyruvate kinase flux that occurs under these conditions (Pryor et al. (1987) Biochem. J. 247, 449-457). (5) An inhibition of pyruvate carboxylase was also implied by a decrease in calculated tissue oxaloacetate concentrations, confirming a role for both enzymes in the inhibition of gluconeogenesis. (6) Whole cell concentrations of effectors of pyruvate carboxylase activity were measured; only the ATP/ADP ratio decreased significantly. (7) Subcellular fractionation studies showed a good correlation between the measured mitochondrial ATP/ADP ratio and rates of gluconeogenesis both in the presence and absence of oleate. (8) A similar correlation could be observed between rates of pyruvate carboxylation and the measured matrix ATP/ADP ratio in isolated liver mitochondria from starved rats. (9) Data are also presented suggesting an additional effect of DCMU on the rate pyruvate carboxylation in situ under some circumstances, mediated by decreases in mitochondrial acetyl-CoA and cytosolic pyruvate concentrations. (10) It is noted that the effects of phenylethylbiguanide (phenformin) on the rate of gluconeogenesis and metabolite profiles in the perfused liver (Cooke et al. (1973) J. Biol. Chem. 248, 5272-5277) are similar to those caused by DCMU, supporting a mitochondrial locus of action for this hypoglycaemic agent.

Adenosine Diphosphate↗
PubMed1980

II. Electrical measurements in the nanosecond range of the charge separation from chloroplasts spread at a heptane-water interface. Application of a novel capacitive electrode.

Spinach chloroplasts are spread at a heptane-water interface. Applying a novel capacitative electrode introduced in the preceding paper (Trissl, H.-W. (1980) Biochim. Biophys. Acta 595, 82-95) the changes of the interface potential induced by single laser flashes are investigated. The following results are obtained: (1) The chloroplasts spread at the interface form a thin layer with asymmetrical orientation. The structural state of this layer is discussed. (2) The photovoltage from the interfacial layer shows similar characteristics as the field-indicating absorption change of chloroplast suspensions, the latter reflecting the photosynthetic primary charge separation: (a) Both can be abolished by addition of 3-(3',4'-dichlorophenyl)-1,1-dimethylurea. (b) About one half of the signals can be reactivated by addition of N-methyl-phenazonium methosulfate. (c) Both signals saturate at low flash light intensities. (d) Both signals can be abolished by background illumination of comparable intensities. (e) Both signals are independent of the ionic strength. (3) The half-rise time of the photovoltage is determined to be less than 3 ns. It is suggested from these results that the photovoltage from the interfacial layer reflects the primary charge separation process in photosynthesis, i.e. the latter is accomplished also within less than 3 ns.

Chloroplasts↗
PubMed1976

Characterization of intracellular esterase A from Bacillus subtilis.

Esterase A (EC 3.1.1.1) obtained by sonic disruption of Bacillus subtilis SR22 (spoA12, trpC2) was purified approximately 400-fold by differential chemical and heating precipitation, DEAE-cellulose chromatography, and Bio-Rad P-150 gel filtration chromatography, with an overall yield of 59%. The purified enzyme hydrolyzed both aliphatic and aromatic acetate esters at substrate concentrations of 0.25 M but did not hydrolyze amino acid esters. Aliphatic alcohols did not inhibit the hydrolysis of p-nitrophenyl acetate; the most potent inhibitors of esterase activity were mercuric chloride, diisopropylfluorophosphate, eserine, and sodium fluoride.

Bacillus subtilis↗
PubMed1976

Properties of the major carboxypeptidase in the larvae of the webbing clothes moth, Tineola bisselliella.

The larvae of the webbing clothes moth, Tineola bisselliella contain two carboxypeptidases (EC 3.4.12-) and one of these has been purified by preparative polyacrylamide gel electrophoresis. Its pH optimum for the hydrolysis of N-benzyloxycarbonyl-glycyl-leucine was pH 7.5-7.7 and its molecular weight as judged by gel filtration was 72 000. It is strongly inhibited by disopropylfluorophosphate, thiol reagents and some metal cations and also by 1:10 phenanthroline but not EDTA. Km and V values for the hydrolysis of 13 N-acyl dipeptides were determined. The enzyme has a strong preference for neutral aliphatic amino acid residues and does not hydrolyse C-terminal proline, arginine or lysine. It is a true carboxypeptidase, requiring an L-amino acid in the C-terminal position, with a free carboxyl group and hydrolysing peptide substrates consecutively from the C-terminal end. Dipeptides are cleaved much more slosly than tripeptides or N-acyl dipeptides.

Animals↗
PubMed1976

Purification and partial characterization of nonspecific lipase from rat pancreas.

Nonspecific lipase (also referred to as micelle lipase and secondary ester hydrolase) has been purified to electrophoretic homogeneity starting from acetone powder of rat pancreas. The purified enzyme is found to have a molecular weight (gel filtration) of 64 000 +/- 2000, and an equivalent weight (titration with E-600) of 65 000. Nonspecific lipase is seen to be very sensitive to inhibition by organophosphates but resistant to quinine. Evidence for the presence of sulfhydryl and imidazole groups essential for activity is presented, and some observations on substrate specificity are made. The purified enzyme appears to lack phosphate groups and lipids, and is unstable under conditions of low ionic strength and/or exposure to 2-mercaptoethanol.

Animals↗