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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↗

Photoinduction kinetics of electrical potential in a single chloroplast as studied with micro-electrode technique.

1. Using single chloroplasts of Peperomia metallica the kinetics of light-induced potential changes were studied. Three kinetic components (the initial fast rise, the decay in the light and the decay in the dark) were found to be characterized by time constants 4, 220 and 60 ms, respectively at light intensity 5000 1x and temperature 18 degrees C. After flash excitation the potential kept on rising for about 10 ms. Cooling of the medium down to 5 degrees C had no effect on the duration of potential rise after the flash. 2. Variations in the medium temperature in the range 2-23 degrees C had little effect on photoresponse magnitude but resulted in significant acceleration of decay in the light. 3. Addition of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (5-)0(-6) M) resulted in suppression of the magnitude of the photoresponse but was not accompanied by any change in the rate of initial rise of potential. 3-(3,4-Dichlorophenyl)-1,1-dimethylurea-inhibited photoresponse could be restored and even enhanced by subsequent addition of N-methylphenazonium methosulfate (10(-4) M). N-Methylphenazonium methosulfate essentially influenced the time course and light-intensity curves of photoresponse. 4. The chloroplast photoresponses were of different time-courses when elicited by red (640 nm) or far red (712 nm) light. This fact as well as an enhancement effect of combined illumination by two intermittent light beams indicate on the interaction of two photosynthetic pigment systems when the photoelectric response was formed. 5. An imposed electrical field resulted in stimulation or suppression of chloroplast photoresponse depending on the polarity of the field. No indications for the existance of "reversal potential" for photoelectric response were obtained. 6. A kinetic scheme of photoresponse formation is proposed, which includes two sequential photochemical reactions of photosynthesis.

Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone↗

The thermodynamic properties of some commonly used oxidation-reduction mediators, inhibitors and dyes, as determined by polarography.

The oxidation-reduction midpoint potentials (Em) of the following compounds have been measured in the range of pH from 3 to 12 by polarography: methyl viologen; benzyl viologen; 2-hydroxy-1,4-naphthoquinone; 2-hydroxy-1,4-anthraquinone; N,N,N',N',-tetramethyl-p-phenylenediamine; 2,3,5,6-tetramethyl-p-phenylenediamine; phenazine; N-methylphenazonium methosulfate; N-methylphenazonium sulfonate methosulfate; N-ethylphenazonium ethosulfate; pyocyanine; neutral red; safranin; phenol red; chlorophenol red; cresol red; bromocresol purple; 2,5-dibromo-3-methyl-6-isopropylbenzoquinone and 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole. Many of these previously assumed to have a simple behavior in this range have proven to be rather more complicated, and several anomalous observations have been reconciled.

Dibromothymoquinone↗

Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. IV. The effects of electron-transport conditions on violaxanthin availability.

1. In isolated chloroplasts of Lactuca sativa var. Manoa, the size of the violaxanthin fraction which is available for de-epoxidation is not directly dependent on electron transport but rather related to the reduced level of some electron carrier between the photosystems. This is concluded from the effects of various electron-transport conditions on violaxanthin availability: Under conditions of electron transport through both photosystems, availability was saturated at a lower electron-transport rate with actinic light at 670 than at 700 nm. Under conditions of electron transport through Photosystem I, availability was smaller for linear electron flow from reduced N-methylphenazonium methosulfate via methylviologen to oxygen than from cyclic electron flow mediated by either N-methylphenazonium methosulfate or 2,6-dichlorophenolindophenol; in addition for linear flow from reduced N-methyphenazonium methosulfate via methylviologen to oxygen, availability increased with decreasing light intensity. 2. The postulated carrier whose reduced level is related to availability seems to be some carrier between plastoquinone and the primary acceptor of Photosystem II or plastoquinone itself. This conclusion follows from the fact that availability increased with increasing light intensity under conditions of electron flow through both photosystems and that 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (greater than or equal to 1 mu M) had no effect on availability, whereas low levels of 3, 3-(3',4'-dichlorophenyl)-1,1-dimethylurea resulted in decreased availability (50 percent decrease at 1 mu M). Furthermore, availability in 3,3-(3',4'-dichlorophenyl)-1,1-dimethylurea-poisoned chloroplasts was fully restored by 2-methyl-1,4-naphtoquinone (menadione) which mediates cyclic electron flow through plastoquinone. 3. Violaxanthin availability was zero in the dark and increased in the light to maximum of 67 percent of the total violazanthin in chloroplasts. It is proposed that this variable violaxanthin availability reflects conformational changes on the internal surface of the thylakoid membrane which result in variable exposure of violaxanthin to the de-epoxidase. The fact that not all of the violaxanthin was available for de-epoxidation may indicate a heterogenous distribution of violaxanthin in the membrane.

Aerobiosis↗

Effect of temperature on proton efflux from isolated chloroplast thylakoids.

Temperature-induced changes in the decay of the light-induced proton gradient of chloroplast thylakoids isolated from chilling-resistant and chilling-sensitive plants have been examined. In the presence of N-methylphenazonium methosulfate, the thylakoids isolated from chilling-resistant barley (cv. Kanby) and pea (cv. Alaska) and chilling-sensitive mung bean (cv. Berken) plants showed temperature-induced changes at approximately 8.6, 13.3, and 14.0 C, respectively. Barley thylakoids assayed in the presence of sodium thiocyanate also showed a change at 8.6 C, whereas with no addition or upon the inclusion of both N-methylphenazonium methosulfate and sodium thiocyanate the change occurred at approximately 11.5 C.Temperature-induced changes in electron transport activities occurred at temperatures approximating those for proton efflux for each of the three plants. These results indicate that temperature has a general effect on thylakoid membranes and that chloroplast thylakoids from chilling-resistant and chilling-sensitive plants have their proton permeability properties affected similarly by temperature.

Journal Article↗

Structural requirements of quinone coenzymes for endogenous and dye-mediated coupled electron transport in bacterial photosynthesis.

Electron transport in continuous light has been investigated in chromatophores of Rhodopseudomonas capsulata. Ala pho+, depleted in ubiquinone-10 and subsequently reconstituted with various ubiquinone homologs and analogs. In addition the restoration of electron transport in depleted chromatophores by the artificial redox compounds N-methylphenazonium methosulfate and N,N,N',N'-tetramethyl-p-phenylenediamine was studied. The following pattern of activities was obtained: (1) Reconstitution of cyclic photophosphorylation with ubiquinone-10 was saturated at about 40 ubiquinone molecules per reaction center. (2) Reconstitution by ubiquinone homologs was dependent on the length of the isoprenoid side chain and the amount of residual ubiquinone in the extracted chromatophores. If two or more molecules of ubiquinone-10 per reaction center were retained, all homologs with a side chain longer than two isoprene units were as active as ubiquinone-10 in reconstitution, and the double bonds in the side chain were not required. If less than two molecules per reaction center remained, an unsaturated side chain longer than five units was necessary for full activity. Plastoquinone, alpha-tocopherol, and naphthoquinones of the vitamin K series were relatively inactive in both cases. (3) All ubiquinone homologs, also ubiquinone-1 and -2, could be reduced equally well by the photosynthetic reaction center, as measured by light-induced proton binding in the presence of antimycin A and uncoupler. Plastoquinone was found to be a poor electron acceptor. (4) Photophosphorylation could be reconstituted by N-methylphenazonium methosulfate as well as by N,N,N',N'-tetramethyl-p-phenylenediamine in an antimycin-insensitive way, if more than two ubiquinones per reaction center remained. These compounds were active also in more extensively extracted particles reconstituted with ubiquinone-1, which itself was inactive.

Adenosine Triphosphate↗

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↗

The effect of complex formation upon the reduction rates of cytochrome c and cytochrome c peroxidase compound II.

The effect of complex formation between ferricytochrome c and cytochrome c peroxidase (Ferrocytochrome-c:hydrogen peroxide oxidoreductase, EC 1.11.1.5) on the reduction of cytochrome c by N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD), reduced N-methylphenazonium methosulfate (PMSH), and ascorbate has been determined at low ionic strength (pH 7) and 25 degrees C. Complex formation with the peroxidase enhances the rate of ferricytochrome c reduction by the neutral reductants TMPD and PMSH. Under all experimental conditions investigated, complex formation with cytochrome c peroxidase inhibits the ascorbate reduction of ferricytochrome c. This inhibition is due to the unfavorable electrostatic interactions between the ascorbate dianion and the negatively charged cytochrome c-cytochrome c peroxidase complex. Corrections for the electrostatic term by extrapolating the data to infinite ionic strength suggest that ascorbate can reduce cytochrome c peroxidase-bound cytochrome c faster than free cytochrome c. Reduction of cytochrome c peroxidase Compound II by dicyanobis(1,10-phenanthroline)iron(II) (Fe(phen)2(CN)2) is essentially unaffected by complex formation between the enzyme and ferricytochrome c at low ionic strength (pH 6) and 25 degrees C. However, reduction of Compound II by the negatively changed tetracyano-(1,10-phenanthroline)iron(II) (Fe(phen)(CN)4) is enhanced in the presence of ferricytochrome c. This enhancement is due to the more favorable electrostatic interactions between the reductant and cytochrome c-cytochrome c peroxidase Compound II complex then for Compound II itself. These studies indicate that complex formation between cytochrome c and cytochrome c peroxidase does not sterically block the electron-transfer pathways from these small nonphysiological reductants to the hemes in these two proteins.

Ascorbic Acid↗

Functional reconstitution of photosystem I reaction center from cyanobacterium Synechocystis sp PCC6803 into liposomes using a new reconstitution procedure.

Photosystem I reaction center from the cyanobacterium Synechocystis sp PCC6803 was reconstituted into phosphatidylcholine/phosphatidic acid liposomes. Liposomes prepared by reversephase evaporation were treated with various amounts of different detergents and protein incorporation was analyzed at each step of the solubilization process. After detergent removal the activities of the resulting proteoliposomes were measured. The most efficient reconstitution was obtained by insertion of the protein complex into preformed liposomes destabilized by saturating amounts of octylglucoside. In the presence of N-methylphenazonium methosulfate and ascorbic acid, liposomes containing the reaction center catalyzed a light-dependent net H+ uptake as measured by the 9-aminoacridine fluorescence quenching and the pH meter. An important benefit of the new reconstitution procedure is that it produces a homogeneous population of large-size proteoliposomes with a low ionic permeability and with a majority inwardly directed H+ transport activity. In optimal conditions, a light-induced delta pH of about 1.8 units could be sustained at 20 degrees C in the presence of valinomycin. In the absence of valinomycin, a "back-pressure" effect of an electrical transmembrane potential decreased both the rate and the extent of the H+ transport. The reaction center was also co-reconstituted with F0F1 H(+)-ATPases from chloroplasts and from the thermophilic bacterium, PS3. The co-reconstituted system was shown to catalyze a light-dependent phosphorylation which could only be measured in the presence of a high concentration of PSI (low lipid/PSI ratios) while no delta pH could be detected.

Ammonium Chloride↗

Spectroscopic properties of the hydroxylase of methane monooxygenase.

The hydroxylase component of methane monooxygenase (EC 1.14.13.25), which catalyzes the oxidation of methane to methanol, has been studied by visible, electron spin resonance and X-ray spectroscopies. The enzyme appears to possess a mu-oxo- or mu-hydroxo-bridged binuclear iron site, with no sulfur ligands to the cluster. Each Fe has 4-6 oxygen (or nitrogen) ligands, at an average distance of 1.92 +/- 0.03 A. The Fe-Fe distance is 3.05 +/- 0.05 A. Essentially all of the irons are in the Fe3+ state as the enzyme is prepared, but reduction with N-methylphenazonium methosulfate generates ESR-detectable states that appear to emanate from mixed-valence binuclear sites. One of these, with gav near 1.85, displays typical Curie law microwave saturation behavior, but the other, gav near 1.73, has a very potent method of spin-relaxation. Together they account for approximately 0.6 spins per molecule.

Binding Sites↗

Physical mechanism for regulation of phosphoenolpyruvate-dependent glucose transport activity in Escherichia coli.

The activity of the phosphoenolpyruvate-dependent glucose phosphotransferase system (PTS) in Escherichia coli is coupled to the oxidation-reduction potential. It is inhibited when the redox potential is increased above -300 mV either via substrate oxidation or via direct addition of oxidizing agents. Depending on the point of addition, dithiothreitol either blocks or reverses these effects. Inhibition occurs at the level of sugar binding to EII. A sulfhydryl group associated with EII activity undergoes reversible oxidation to, presumably, a disulfide, resulting in the conversion of EII from a reduced, high-affinity form to an oxidized, low-affinity form which has a 10(2)-10(3) times lower affinity for the sugar. An identical change in affinity occurs as the result of the generation of a delta mu H+ during the oxidation of reduced N-methylphenazonium methosulfate or nicotinamide adenine dinucleotide. In this case, uncouplers and ionophores reverse the change. A mechanism is proposed in which the electrical potential difference across the membrane regulates the glucose PTS by shifting the midpoint potential of the EII-associated redox transition to more negative values. As a result, EII is converted to the oxidized, low-affinity state in the presence of a delta mu H+.

Biological Transport, Active↗

Electron transfer in reaction center core complexes from the green sulfur bacteria Prosthecochloris aestuarii and Chlorobium tepidum.

Electron transfer in reaction center core (RCC) complexes from the green sulfur bacteria Prosthecochloris aestuarii and Chlorobium tepidum was studied by measuring flash-induced absorbance changes. The first preparation contained approximately three iron-sulfur centers, indicating that the three putative electron acceptors F(X), F(A), and F(B) were present; the Chl. tepidum complex contained on the average only one. In the RCC complex of Ptc. aestuarii at 277 K essentially all of the oxidized primary donor (P840(+)) created by a flash was rereduced in several seconds by N-methylphenazonium methosulfate. In RCC complexes of Chl. tepidum two decay components, one of 0.7 ms and a smaller one of about 2 s, with identical absorbance difference spectra were observed. The fast component might be due to a back reaction of P840(+) with a reduced electron acceptor, in agreement with the notion that the terminal electron acceptors, F(A) and F(B), were lost in most of the Chl. tepidum complexes. In both complexes the terminal electron acceptor (F(A) or F(B)) could be reduced by dithionite, yielding a back reaction of 170 ms with P840(+). At 10 K in the RCC complexes of both species P840(+) was rereduced in 40 ms, presumably by a back reaction with F(X)(-). In addition, a 350 micros component occurred that can be ascribed to decay of the triplet of P840, formed in part of the complexes. For P840(+) rereduction a pronounced temperature dependence was observed, indicating that electron transfer is blocked after F(X) at temperatures below 200 K.

Chlorobi↗

Preparation and properties of chloroplasts depleted of chloroplast coupling factor 1 by sodium bromide treatment.

Chloroplasts were treated with 2 m sodium bromide. The resulting particles lost their ATPase activity and chloroplast coupling factor 1 subunits were detected in the supernatant by means of gel electrophoresis and specific antibodies. The chloroplast coupling factor 1 depleted particles show high rates of Hill reaction with pH optimum shifted toward lower pH. The sodium bromide treatment also abolished the light-induced proton uptake. In the presence of N-methylphenazonium methosulfate light-induced proton release, insensitive to uncouplers, was observed. Addition of dicyclohexylcarbodiimide reversed the light-induced pH changes to the normal proton uptake and increased the pH optimum of the Hill reaction.

Journal Article↗

Reconstitution of photosynthetic energy conservation. I. Proton movements in liposomes containing reaction center of photosystem I from spinach chloroplasts.

A preparation of reaction centers of photosystem I from spinach chloroplasts was incorporated into lipid vesicles by sonication. Incorporation was tested by chromatography on Sepharose-4B, by comparison of the elution profiles of photosystem-I reaction center liposomes and of free reaction centers. In the presence of reduced N-methylphenazonium methosulfate the reaction center liposomes catalyzed net proton extrusion in the light, but at the same time showed light-induced quenching of 9-aminoacridine fluorescence, with similar extent and kinetics as known for chloroplasts. We conclude that we are dealing with two vesicle populations, one right side-out and one inside-out with respect to the orientation of the incorporated reaction center complex. Net proton movements are influenced by the nature of the cations present in the suspending medium, and the possibilities for effects of surface charge on these movements are discussed.

Aminoacridines↗

Demonstration of rhodanese activity in polyacrylamide gels.

Rhodanese activity from crude extracts of Thiobacillus sp. strain IV-85 was demonstrated in polyacrylamide gels after incubation in the reaction mixture by staining with dichloroindophenol in the presence of methylphenazonium methosulfate. The sensitivity of the staining system was found to be 8 x 10 moles of sulfite.

Journal Article↗

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↗