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Evidence against proton gradient formation being the cause of chlorophyll fluorescence quenching by N-methylphenazonium methosulfate.

In strong illumination, 3-(3, 4-dichlorophenyl)-1,1-dimethylurea (DCMU)-poisoned chloroplasts exhibit a high yield of chlorophyll fluorescence while P-700 turnover, proton uptake, and phosphorylation are inhibited and a pH gradient is undectectable. When 10muM N-methylphenazonium methosulfate (PMS) is included, the fluorescence yield in light is substantially reduced, and when 100 muM ascorbate is also included, the yield is diminished approximately to the level in darkness. Only very slight increases in P-700 turnover and proton uptake (but no detectable pH gradient) accompany the fluorescence yield decline. When 10muM PMS and 15 mM ascorbate are added to poisoned chloroplasts (the oxygen concentration being greatly reduced), P-700 turnover, proton uptake, the pH gradient and phosphorylation all reach high levels. In this case, the yield of chlorophyll fluorescence is low and is the same in both light and dark. Further addition of an uncoupler eliminates proton uptake, the pH gradient and phosphorylation but does not significantly elevate the fluorescence yield. From these observations we suggest that, in DCMU-poisoned chloroplasts, the fluorescence quenching with PMS occurrs by a mechanism unrelated to the generation of a phosphyorylation potential. With chloroplasts unpoisoned by DCMU, PMS quenches fluorescence and considerably stimulates proton uptake, the pH gradient and phosphorylation. However, in this case, PMS serves to restore net electron transport.

Ammonia

Interaction of oxidized and reduced N-methylphenazonium methosulfate (PMS) with photosystem II.

In 3-(3,4-dicholorophenyl)-1,1-dimethylurea (DCMU) poisoned chloroplasts, the restoration of the fluorescence induction is presumed to be due to a back reaction of the reduced primary acceptor (Q-) and the oxidized primary donor (Z+) of Photosystem II. Carbonylcyanide m-chlorophenylhydrazone (CCCP) is known to inhibit this back reaction. The influence of reduced N-methylphenazonium methosulfate (PMS) in the absence of CCCP and of oxidized PMS in the presence of CCCP on the back reaction was investigated and the following results were obtained: (1) Reduced PMS at the concentration of 1 muM inhibits the back reaction as effectively as hydroxylamine, suggesting an electron donating function of reduced PMS for System II. (2) The inhibition of the back reactionby CCCP is regenerated to a high degree by oxidized PMS which led to assume a cyclic System II electron flow catalysed by PMS. (3) At concentrations of reduced PMS higher than 1 muM it is shown that both the fast initial emission and more significantly the variable emission are quenched.

Carbonyl Cyanide m-Chlorophenyl Hydrazone

The stimulation of photophosphorylation and ATPase by artificial redox mediators in chromatophores of Rhodopseudomonas capsulata at different redox potentials.

(1) Inhibition of cyclic phosphorylation in chromatophores of Rhodopseudomonas capsulata by antimycin A can be fully reversed by artificial redox mediators, provided the ambient redox potential is maintained around 200 mV. The redox mediator need not be a hydrogen carrier in its reduced form, N-methyl-phenazonium methosulfate and N,N,N',N'-tetramethyl-p-phenylenediamine being equally effective. However, the mediator needs to be lipophilic. Endogenous cyclic phosphorylation is fastest around 130 mV. A shift to 200 mV can also be observed if high concentrations of artificial redox mediator are present in the absence of antimycin. (2) ATPase activity of Rhodopseudomonas capsulata, in the light as well as in the dark, activated or not activated by inorganic phosphate, can also be stimulated by N-methylphenazonium methosulfate. This stimulation is highest at redox potentials between 60 to 80 mV and is sensitive to antimycin A. In this case N,N,N',N-tetramethyl-p-phenylenediamine is much less effective.

Adenosine Triphosphatases

A comparison of electron transport and photophosphorylation systems of Rhodopseudomonas capsulata and Rhodospirillum rubrum. Effects of antimycin A and dibromothymoquinone.

The photophosphorylation systems of Rhodopseudomonas capsulata and Rhodospirillum rubrum chromatophores have been compared in respect to the effects of artificial electron carriers [N-methylphenazonium methosulfate (PMS) and diaminodurene], reducing agents (ascorbate in particular), and various quinones in the absence and presence of the electron transport inhibitors antimycin A and dibromothymoquinone (DBMIB). In addition, the effects of both inhibitors on photosynthetic electron transport through cytochromes b and c has been followed. From the results obtained, it appears that in both organisms: a) ubiquinone functions as an electron carrier between the cytochromes, and b) both antimycin A and DBMIB inhibit cyclic electron flow in the segment...cytochrome b leads to ubiquinone leads to cytochrome c..., but at different sites. The systems apparently differ mainly in respect to the nature of the electron flow by-pass "shunt" that is evoked in the presence of PMS; thus, in R. rubrum, PMS catalyzes a shunt that by-passes both cytochrome b and ubiquinone, whereas in Rps. capsulata the PMS shunt seems to circumvent only ubiquinone.

Antimycin A

Method for isolation of Escherichia coli mutants with defects in the proton-translocating sector of the membrane adenosine triphosphatase complex.

A technique for selecting mutants of Escherichia coli in which the proton-translocating sector of the adenosine triphosphatase (ATPase) complex has been inactivated is reported. The procedure uses a strain of E. coli (NR-70) lacking the extrinsic (F1) sector of the ATPase complex and which in consequently permeable to protons (B. P. Rosen, J. Bacteriol. 116:1124--1129, 1973). After growing strain NR-70 under noninducing conditions for the lac operon, cells were mutagenized and plated on minimal medium containing low concentrations of lactose. Several mutants of strain NR-70 were isolated as large colonies on these plates, apparently because they could concentrate lactose more efficiently. A description of one of the mutants, strain KW-1, is reported here. The most distinguishing difference in growth properties of the two strains was that, when transferred to medium containing low concentrations of lactose, strain KW-1 induced the lac operon with a shorter lag time than strain NR-70. The mutation in strain KW-1 leading to more rapid growth on lactose was cotransducible with the asn and unc loci, at 83 min on the E. coli genetic map. Intact cells of strain KW-1 actively transported L-proline as well as did wild-type cells, whereas cells of strain NR-70 were markedly deficient in L-proline transport. The improvement in the transport capacity of strain KW-1 correlated with a marked decrease in proton permeability relative to that of strain NR-70. Based on an acid-base pulse technique that measured the proton conductance of the membranes of intact cells, strain NR-70 was at least 10 times more permeable to protons than was the wild type, whereas strain KW-1 was only 2 times more permeable. The transport properties and proton conductance were also compared with membrane vesicles prepared by osmotic shock. With either D-lactate or ascorbate-N-methylphenazonium methosulfate as respiratory substrates, vesicles of strain KW-1 transported L-proline much more rapidly than did vesicles of strain NR-70, but still at rates less rapid than those of the wild type. The passive proton conductance of the membrane vesicles was quantitated by measuring the rate of H+ influx into vesicles in response to a valinomycin-generated K+ diffusion potential. The proton permeability of vesicles of strain KW-1 was reduced 1.5-fold relative to vesicles of strain NR-70, but these vesicles were still four times more permeable to protons than was the wild type. Vesicles of strain KW-1 corresponded to wild-type vesicles treated with 0.5 micrometer carbonylcyanide m-chlorophenylhydrazone (CCCP) and vesicles of strain NR-70 corresponded to wild-type vesicles treated with 1.4 micrometer CCCP. Treatment of wild-type vesicles with these concentrations of CCCP caused decreases in transport comparable to those observed in the mutants. Strain KW-1 lacked ATPase activity. Cross-reacting material to F1-ATPase was not found in strain KW-1 by double immunodiffusion analysis.

Adenosine Triphosphatases

[The mechanism of the tetrazolium reduction and the effect of phenazinmethosulfate (author's transl)].

Modern results of the literature form the basis for the presentation of a scheme which shows the reduction of tetrazolium salts and the action of phenazine methosulfate under histochemical conditions. The reduction of tetrazolium salts passes the radical state and it hapens principally on the niveau of the flavin proteins and the ubiquinone. The importance of the superoxide radical for the reduction of tetrazolium salts under aerobic conditions is emphasized.

Aerobiosis

Phototaxis and membrane potential in the photosynthetic bacterium Rhodospirillum rubrum.

Cells of the photosynthetic bacterium Rhodospirillum rubrum cultivated anaerobically in light show phototaxis. The behavior of individual cells in response to the phenomenon is reversal(s) of the swimming direction when the intensity of the light available to them abruptly decreases. The tactic response was inhibited by antimycin, an inhibitor of the photosynthetic electron transfer system. The inhibitory effect of antimycin was overcome by phenazine methosulfate. Motility of the cells was not impaired by antimycin under aerobic conditions. Valinomycin plus potassium also inhibited their phototactic response; however, valinomycin or potassium alone had no effect. A change in membrane potential of the cells was measured as an absorbance change of carotenoid. Changes in the membrane potential caused by "on-off" light were prevented by antimycin and by valinomycin plus potassium, but not by antimycin plus phenazine methosulfate nor valinomycin or potassium alone. The results indicated that the phototactic response of R. rubrum is mediated by a sudden change in electron flow in the photosynthetic electron transfer system, and that the membrane potential plays an important role in manifestation of the response.

Aerobiosis

Generation of free radicals from phenazine methosulfate in Trypanosoma cruzi epimastigotes.

A significant growth inhibition of Trypanosoma cruzi epimastigotes by phenazine methosulfate (PMS) was observed in Warren's medium. This toxic activity could be related to the following parameters: a) formation of phenazinium free radical, b) generation of superoxide anion in intact cells incubated with PMS, and c) PMS also increased significantly the rate of O2- generation in epimastigotes mitochondrial and microsomal fractions using NADH as electron donor.

Electron Spin Resonance Spectroscopy

Methylamine dehydrogenase of Pseudomonas sp. J. Purification and properties.

Methylamine dehydrogenase was purified in a homogeneous form from methylamine-grown Pseudomonas sp. J. The specific activity of the purified enzyme was 5.19 at 19 degrees C. The molecular weight was estimated to be 105 000, and the enzyme was composed of two kinds of subunit with molecular weights of 40 000 and 13 000, respectively. The enzyme contained little phosphorus, iron and copper. The enzyme had absorption maxima at 278, 330, 430 and 460 nm (shoulder). On addition of methylamine, the peaks at 430 and 460 nm decreased, while that at 330 nm increased. Primary amines served as substrates, but secondary and tertiary amines did not. Phenazine methosulfate was the most effective electron acceptor and oxygen was ineffective. The enzyme was inhibited by carbonyl reagents, cuprizone and HgCl2 but not by other chelators or sulfhydryl reagents. Some of other physical and biochemical properties of the enzyme were studied. These results show that the enzyme purified from Pseudomonas sp. J is essentially similar to the enzyme obtained from Pseudomonas AM1, although it differs slightly in some properties.

Amino Acids

Pentose cycle activity of the isolated perfused rat lung.

Pentose cycle activity was estimated in isolated rat lungs under varying conditions of glucose oxidation. Lungs were perfused for 100-120 min with a Krebs-Ringer-bicarbonate buffer, pH 7.4, containing 1-14C- or 6-14C-labeled glucose and ventilated with 95% O2:5% CO2. Based on 14C specific yields in either 14CO2 or perfusate lactate plus pyruvate, pentose cycle flux in control lungs was 5.3 mumol of glucose per hour per gram dry weight (11-12% of glucose utilization). Pentose cycle activity was unaltered by perfusion with 0.8 mM 2,4-dinitrophenol. Perfusion with phenazine methosulfate, an artificial hydrogen acceptor, resulations of the pentose cycle based on 14C yields in tissue lipids (both the fatty acid and deacylated fractions) gave values 2-3 times higher than measurements based on 14CO2. This study indicates that pentose cycle activity in the lung accounts for a significant fraction of glucose utilization and this pathway readily responds to metabolic perturbation.

Animals

The pentose phosphate pathway in developing chick cornea.

Embryonic chick corneas at different stages of development were evaluated for activity of the pentose phosphate pathway. The appearance of activity was concurrent with the onset of corneal transperancy (stage 40). Highest values were found after complete transparency is achieved (stage 45 and after hatching). Phenazine methosulfate, an artificial electron acceptor, increased activity at all stages studied even before endogenous activity was measurable; however, no increase in glucose uptake was observed. Thus, the enzymes for the pathway are present at early stages (i.e., stage 38 and 40) although in latent form. The pathway probably functions in the developing cornea to generate NADPH rather than sugar moieties for macromolecular incorporation.

Age Factors

Interaction of a coupling factor from Rhodospirillum rubrum with coupling factor deficient chromatophores.

A coupling factor necessary for the photophosphorylation and Mg2+-ATPase activities in Rhodospirillum rubrum chromatophores has been separated from these particles. Although the redox potential of coupling factor deficient chromatophores is slightly more oxidized than of the control, the addition of the coupling factor for reconstitution does not alter the redox potential. Phenazine methosulfate cannot restore or significantly enhance the photophosphorylation activities of uncoupled or reconstituted chromatophores compared to the control. The coupling factor can bind to coupling factor deficient membranes without addition of magnesium ions and thus restore the photophosphorylation and Mg2+-ATPase activities of these vesicles. The Ca2+-ATPase in the coupling factor preparation shows binding characteristics similar to those of the coupling factor.

Adenosine Triphosphatases

Acceleration of tetrazolium reduction by bacteria.

Conditions were assessed which would permit more rapid recognition of bacterial growth than has been previously reported using tetrazolium salts. Microtitration trays were used. 2-(p-Iodophenyl)-3(p-nitrophenyl)-5-phenyltetrazolium chloride is rapidly reduced by respiring cells in tissue homogenates but is more toxic than other tetrazoliums when added to growing bacterial cultures. Phenazine methosulfate (PMS), an intermediate electron carrier, potentiates tetrazolium reduction. Growth was readily detected by the addition of these compounds after 3 to 4 h of incubation in Schaedler broth. The final concentration prior to addition to tray wells was 1.0 mg/ml for 2-(p-iodophenyl)-3(p-nitrophenyl)-5-phenyltetrazolium chloride and 0.06 mg/ml for PMS. Addition of 0.5 to 0.8 g of agar per liter of broth enhanced subsequent tetrazolium reduction.

Bacteria