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PubMed2002

Characterization of a low redox potential laccase from the basidiomycete C30.

A new exocellular laccase was purified from the basidiomycete C30. LAC2 is an acidic protein (pI = 3.2) preferentially produced upon a combined induction by copper and p-hydroxybenzoate. The spectroscopic signature (UV/visible and EPR) of this isoform is typical of multicopper oxidases, but its enzymatic and physico-chemical properties proved to be markedly different from those of LAC1, the constitutive laccase previously purified from the same organism. In particular, the LAC2 kcat values observed for the oxidation of the substrates syringaldazine (kcat = 65 600 min-1), ABTS (2,2-azino-bis-[3-ethylthiazoline-6-sulfonate] (kcat = 41 000 min-1) and guaiacol (kcat = 75 680 min-1) are 10-40 times those obtained with LAC1 and the redox potential of its T1 copper is 0.17 V lower than that of LAC1 (E degrees = 0.73 V). This is the first report on a single organism producing simultaneously both a high and a low redox potential laccase. The cDNA, clac2, was cloned and sequenced. It encodes a protein of 528 amino acids that shares 69% identity (79% similarity) with LAC1 and 81% identity (95% similarity) with Lcc3-2 from Polyporus ciliatus (AF176321-1), its nearest neighbor in database. Possible reasons for why this basidiomycete produces, in vivo, enzyme forms with such different behaviors are discussed.

Azides↗
PubMed1986

Regulation of dehydrogenases/one-electron transferases by modification of flavin redox potentials. Effect of product binding on semiquinone stabilization in yeast flavocytochrome b2.

Spectroscopic and potentiometric measurements have been carried out, at room temperature, during anaerobic titrations of Hansenula anomala L-lactate cytochrome c oxidoreductase (or flavocytochrome b2) both in the presence and in the absence of pyruvate (the physiological reaction product). Under the same conditions, the flavin spectral contribution was estimated and the flavosemiquinone proportion was directly determined by electron paramagnetic resonance measurements. In the present study, we show the visible light absorption and paramagnetic characteristics of the flavin radical at 18 degrees C and also the dramatic effect of pyruvate on the redox potential of each monoelectronic couple of the flavin. Thermodynamic stabilization of the semiquinone form, in the presence of pyruvate, is interpreted as a mode of regulation of flavocytochrome b2 activity. Taking into account that analogous controls have been observed with two other flavoenzymes belonging to this class of dehydrogenases/one-electron transferases, we suggest that redox potential modulation could be a type of regulation effective for the whole class of enzymes in which a semiquinone is an obligate intermediate.

Electron Spin Resonance Spectroscopy↗
PubMed1999

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors.

The flavoenzyme d-aspartate oxidase from beef kidney (DASPO, EC 1.4. 3.1) has been overexpressed in Escherichia coli. A purification procedure, faster than the one used for the enzyme from the natural source (bDASPO), has been set up yielding about 2 mg of pure recombinant protein (rDASPO) per each gram of wet E. coli paste. rDASPO has been shown to possess the same general biochemical properties of bDASPO, except that the former contains only FAD, while the latter is a mixture of two forms, one active containing FAD and one inactive containing 6-OH-FAD (9-20% depending on the preparation). This results in a slightly higher specific activity (about 15%) for rDASPO compared to bDASPO and in facilitated procedures for apoprotein preparation and reconstitution. Redox potentials of -97 mV and -157 mV were determined for free and l-(+)-tartrate complexed DASPO, respectively, in 0.1 M KPi, pH 7.0, 25 degrees C. The large positive shift in the redox potential of the coenzyme compared to free FAD (-207 mV) is in agreement with similar results obtained with other flavooxidases. rDASPO has been used to assess a possible oxidative activity of the enzyme towards a number of compounds used as agonists or antagonists of neurotransmitters, including d-aspartatic acid, d-glutamic acid, N-methyl-d-aspartic acid, d,l-cysteic acid, d-homocysteic acid, d, l-2-amino-3-phosphonopropanoic acid, d-alpha-aminoadipic acid, d-aspartic acid-beta-hydroxamate, glycyl-d-aspartic acid and cis-2, 3-piperidine dicarboxylic acid. Kinetic parameters for each substrate in 50 mM KPi, pH 7.4, 25 degrees C are reported.

Amino Acid Oxidoreductases↗
PubMed1998

Site-directed mutations in fungal laccase: effect on redox potential, activity and pH profile.

A Myceliophthora thermophila laccase and a Rhizoctonia solani laccase were mutated on a pentapeptide segment believed to be near the type-1 Cu site. The mutation L513F in Myceliophthora laccase and the mutation L470F in Rhizoctonia laccase took place at a position corresponding to the type-1 Cu axial methionine (M517) ligand in Zucchini ascorbate oxidase. The triple mutations V509L,S510E,G511A in Myceliophthora laccase and L466V,E467S,A468G in Rhizoctonia laccase involved a sequence segment whose homologue in ascorbate oxidase is flanked by the M517 and a type-1 Cu-ligating histidine (H512). The single mutation did not yield significant changes in the enzymic properties (including any significant increase in the redox potential of the type-1 Cu). In contrast, the triple mutation resulted in several significant changes. In comparison with the wild type, the Rhizoctonia and Myceliophthora laccase triple mutants had a phenol-oxidase activity whose pH optimum shifted 1 unit lower and higher, respectively. Although the redox potentials were not significantly altered, the Km, kcat and fluoride inhibition of the laccases were greatly changed by the mutations. The observed effects are interpreted as possible mutation-induced structural perturbations on the molecular recognition between the reducing substrate and laccase and on the electron transfer from the substrate to the type-1 Cu centre.

Amino Acid Sequence↗
PubMed1997

Ca2+ dependence of gluconeogenesis stimulation by glucagon at different cytosolic NAD(+)-NADH redox potentials.

The influence of Ca2+ on hepatic gluconeogenesis was measured in the isolated perfused rat liver at different cytosolic NAD(+)-NADH potentials. Lactate and pyruvate were the gluconeogenic substrates and the cytosolic NAD(+)-NADH potentials were changed by varying the lactate to pyruvate ratios from 0.01 to 100. The following results were obtained: a) gluconeogenesis from lactate plus pyruvate was not affected by Ca(2+)-free perfusion (no Ca2+ in the perfusion fluid combined with previous depletion of the intracellular pools); gluconeogenesis was also poorly dependent on the lactate to pyruvate ratios in the range of 0.1 to 100; only for a ratio equal to 0.01 was a significantly smaller gluconeogenic activity observed in comparison to the other ratios. b) In the presence of Ca2+, the increase in oxygen uptake caused by the infusion of lactate plus pyruvate at a ratio equal to 10 was the most pronounced one; in Ca(2+)-free perfusion the increase in oxygen uptake caused by lactate plus pyruvate infusion tended to be higher for all lactate to pyruvate ratios; the most pronounced difference was observed for lactate/pyruvate ratio equal to 1. c) In the presence of Ca2+ the effects of glucagon on gluconeogenesis showed a positive correlation with the lactate to pyruvate ratios; for a ratio equal to 0.01 no stimulation occurred, but in the 0.1 to 100 range stimulation increased progressively, producing a clear parabolic dependence between the effects of glucagon and the lactate to pyruvate ratio. d) In the absence of Ca2+ the relationship between the changes caused by glucagon in gluconeogenesis and the lactate to pyruvate ratio was substantially changed; the dependence curve was no longer parabolic but sigmoidal in shape with a plateau beginning at a lactate/pyruvate ratio equal to 1; there was inhibition at the lactate to pyruvate ratios of 0.01 and 0.1 and a constant stimulation starting with a ratio equal to 1; for the lactate to pyruvate ratios of 10 and 100, stimulation caused by glucagon was much smaller than that found when Ca2+ was present. e) The effects of glucagon on oxygen uptake in the presence of Ca2+ showed a parabolic relationship with the lactate to pyruvate ratios which was closely similar to that found in the case of gluconeogenesis; the only difference was that inhibition rather than stimulation of oxygen uptake was observed for a lactate to pyruvate ratio equal to 0.01; progressive stimulation was observed in the 0.1 to 100 range. f) In the absence of Ca2+ the effects of glucagon on oxygen uptake were different; the dependence curve was sigmoidal at the onset, with a well-defined maximum at a lactate to pyruvate ratio equal to 1; this maximum was followed by a steady decline at higher ratios; at the ratios of 0.01 and 0.1 inhibition took place; oxygen uptake stimulation caused by glucagon was generally lower in the absence of Ca2+ except when the lactate to pyruvate ratio was equal to 1. The results of the present study demonstrate that stimulation of gluconeogenesis by glucagon depends on Ca2+. However, Ca2+ is only effective in helping gluconeogenesis stimulation by glucagon at highly negative redox potentials of the cytosolic NAD(+)-NADH system. The triple interdependence of glucagon-Ca(2+)-NAD(+)-NADH redox potential reveals highly complex interrelations that can only be partially understood at the present stage of knowledge.

Animals↗
PubMed2002

A transient exchange of the photosystem II reaction center protein D1:1 with D1:2 during low temperature stress of Synechococcus sp. PCC 7942 in the light lowers the redox potential of QB.

Upon exposure to low temperature under constant light conditions, the cyanobacterium Synechococcus sp. PCC 7942 exchanges the photosystem II reaction center D1 protein form 1 (D1:1) with D1 protein form 2 (D1:2). This exchange is only transient, and after acclimation to low temperature the cells revert back to D1:1, which is the preferred form in acclimated cells (Campbell, D., Zhou, G., Gustafsson, P., Oquist, G., and Clarke, A. K. (1995) EMBO J. 14, 5457-5466). In the present work we use thermoluminescence to study charge recombination events between the acceptor and donor sides of photosystem II in relation to D1 replacement. The data indicate that in cold-stressed cells exhibiting D1:2, the redox potential of Q(B) becomes lower approaching that of Q(A). This was confirmed by examining the Synechococcus sp. PCC 7942 inactivation mutants R2S2C3 and R2K1, which possess only D1:1 or D1:2, respectively. In contrast, the recombination of Q(A)(-) with the S(2) and S(3) states did not show any change in their redox characteristics upon the shift from D1:1 to D1:2. We suggest that the change in redox properties of Q(B) results in altered charge equilibrium in favor of Q(A). This would significantly increase the probability of Q(A)(-) and P680(+) recombination. The resulting non-radiative energy dissipation within the reaction center of PSII may serve as a highly effective protective mechanism against photodamage upon excessive excitation. The proposed reaction center quenching is an important protective mechanism because antenna and zeaxanthin cycle-dependent quenching are not present in cyanobacteria. We suggest that lowering the redox potential of Q(B) by exchanging D1:1 for D1:2 imparts the increased resistance to high excitation pressure induced by exposure to either low temperature or high light.

Cyanobacteria↗
PubMed2003

Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli. Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials.

On the basis of amino acid sequences and crystal structures of similar enzymes, it is proposed that Met95 of the heme-regulated phosphodiesterase from Escherichia coli (Ec DOS) acts as a heme axial ligand. In accordance with this proposal, the Soret and visible optical absorption and magnetic circular dichroism spectra of the Fe(II) complexes of the Met95Ala and Met95Leu mutant proteins indicate that these complexes are five-coordinated high-spin, suggesting that Met95 is an axial ligand for the Fe(II) complex. However, the Fe(III) complexes of these mutants are six-coordinated low-spin, like the wild-type enzyme. The latter spectral findings are inconsistent with the proposal that the axial ligand to the Fe(III) heme is Met95. To determine the possibility of a redox-dependent ligand switch in Ec DOS, we further analyzed Soret CD spectra and redox potentials, which provide direct evidence on the environmental structure of the heme protein. CD spectra of Fe(III) Met95 mutants were all different from those of the wild-type protein, suggesting indirect coordination of Met95 to the Fe(III) wild-type heme. The redox potentials of the Met95Leu, Met95Ala and Met95His mutants were considerably lower than that of the wild-type enzyme (+70 mV) at -1, -26, and -122 mV vs. SHE, respectively. Thus, it is reasonable to speculate that water (or hydroxy anion) interacting with Met95, rather than Met95 itself, is the axial ligand to the Fe(III) heme.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1984

Electron transfer between flavodoxin semiquinone and c-type cytochromes: correlations between electrostatically corrected rate constants, redox potentials, and surface topologies.

We have measured the ionic strength dependence of the rate constants for electron transfer from the semiquinone of Clostridium pasteurianum flavodoxin to 12 c-type cytochromes and several inorganic oxidants using stopped-flow methodology. The experimental data were fit quite well by an electrostatic model that represents the interaction domains as parallel disks with a point charge equal to the charge within this region of the protein. The analysis provides an evaluation of the electrostatic interaction energy and the rate constant at infinite ionic strength (k affinity). The electrostatic charge on the oxidant within the interaction site can be obtained from the electrostatic energy, and for most of those reactants for which structures are available, the results are in good agreement with expectation. The k affinity values were found to correlate with redox potential differences, as expected from the theory of adiabatic (or nonadiabatic) outer-sphere electron-transfer reactions. Deviations from the theoretical curves are interpreted in terms of the influence of surface topology on reaction rate constants. In general, we find that electrostatic effects, steric influences, and redox potential all exert a much larger effect on reaction rate constants for the flavodoxin-cytochrome system than has been previously observed for free flavin-cytochrome interactions. The implications of this for determining biological specificity are discussed.

Clostridium↗
PubMed1999

A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: implications for the evolution of energy-conserving heme-copper oxidases.

Bacterial nitric oxide reductase (NOR) catalyzes the two-electron reduction of nitric oxide to nitrous oxide. It is a highly diverged member of the superfamily of heme-copper oxidases. The main feature by which NOR is distinguished from the heme-copper oxidases is the elemental composition of the active site, a dinuclear center comprised of heme b(3) and non-heme iron (Fe(B)). The visible region electronic absorption spectrum of reduced NOR exhibits a maximum at 551 nm with a distinct shoulder at 560 nm; these are attributed to Fe(II) heme c (E(m) = 310 mV) and Fe(II) heme b (E(m) = 345 mV), respectively. The electronic absorption spectrum of oxidized NOR exhibits a characteristic shoulder around 595 nm that exhibits complex behavior in equilibrium redox titrations. The first phase of reduction is characterized by an apparent shift of the shoulder to 604 nm and a decrease in intensity. This is due to reduction of Fe(B) (E(m) = 320 mV), while the subsequent bleaching of the 604 nm band represents reduction of heme b(3) (E(m) = 60 mV). This separation of redox potentials (>200 mV) allows the enzyme to be poised in the three-electron reduced state for detailed spectroscopic examination of the Fe(III) heme b(3) center. The low midpoint potential of heme b(3) represents a thermodynamic barrier to the complete (two-electron) reduction of the dinuclear center. This may avoid formation of a stable Fe(II) heme b(3)-NO species during turnover, which may be an inhibited state of the enzyme. It would also appear that the evolution of significant oxygen reducing activity by heme-copper oxidases was not simply a matter of the substitution of copper for non-heme iron in the dinuclear center. Changes in the protein environment that modulate the midpoint redox potential of heme b(3) to facilitate both complete reduction of the dinuclear center (a prerequisite for oxygen binding) and rapid heme-heme electron transfer were also necessary.

Circular Dichroism↗
PubMed1969

THE EFFECT OF REDOX POTENTIAL ON P870 FLUORESCENCE IN REACTION CENTERS FROM Rhodopseudomonas spheroides.

We have prepared photosynthetic reaction centers from Rhodopseudomonas spheroides and have studied the fluorescence of the photochemical electron donor, P870. The yield of this fluorescence rises at low redox potential, presumably because the photochemical electron acceptor becomes reduced and the photochemical utilization of excitation energy is then prevented. The redox titration curve for this increase in the fluorescence has a shape corresponding to the transfer of one electron. The midpoint potential is -0.05 volt, independent of the pH from 6.5 to 8.8. The amplitude of a light-induced absorbance change at 280 nanometers varies with redox potential and shows, at pH 7.5, a midpoint potential of 0.00 volt. These studies indicate that the primary photochemical electron acceptor is not ubiquinone and is not the substance responsible for the absorbance change at 280 nanometers.

Journal Article↗
PubMed2001

Selective activation of mitomycin A by thiols to form DNA cross-links and monoadducts: biochemical basis for the modulation of mitomycin cytotoxicity by the quinone redox potential.

Mitomycin A (MA) but not mitomycin C (MC) cross-linked linearized (32)P-pBR322 DNA in the presence of dithiothreitol (DTT) or glutathione (GSH), as shown by a sensitive DNA cross-link assay. Incubation of calf-thymus DNA with MA and DTT or mercaptoethanol (MER) resulted in the formation of MA-DNA adducts, which were isolated from nuclease digests of the drug-DNA complexes by HPLC. The adducts were characterized by their UV absorption spectra, electrospray ionization mass spectrometry (ESIMS), and facile conversion from 7-methoxy- to 7-amino-substituted mitosene type adducts upon 10% NH(4)OH treatment, which were identical with known adducts of MC. Both DNA interstrand and intrastrand cross-link adducts, linking two deoxyguanosine residues at N(2), as well as several deoxyguanosine-N(2) monoadducts of MA, were identified. No DNA adducts were formed with MC under the same conditions. A specificity of DNA cross-link formation for the CpG sequence was observed using 12-mer synthetic oligodeoxyribonucleotides as substrates and as DNA sequence models, in analogy to the known CpG sequence specificity of MC-induced DNA cross-links. MA is known to be more cytotoxic by 2-3 orders of magnitude than MC, and this property correlates with redox potentials of MA (-0.19 V) and MA analogues that are higher than those of MC (-0.40 V) and its analogues. It is suggested that the biochemical basis for the higher cytotoxic potency of MA is MA's propensity to be reductively activated by cellular thiols while MC is resistant to thiol activation. This distinction is probably derived from the large difference between the quinone redox potentials of the two drugs.

Ammonium Hydroxide↗
PubMed2000

Insulin increases NO-stimulated guanylate cyclase activity in cultured VSMC while raising redox potential.

Insulin acutely stimulates cyclic guanosine monophosphate (cGMP) production in primary confluent cultured vascular smooth muscle cells (VSMC) from canine femoral artery, but the mechanism is not known. These cells contain the inducible isoform of nitric oxide (NO) synthase (iNOS), and insulin-stimulated cGMP production in confluent cultured cells is blocked by the NOS inhibitor, N(G)-monomethyl-L-arginine (L-NMMA). In the present study, it is shown that iNOS is also present in freshly dispersed VSMC from this artery, indicating that iNOS expression in cultured VSMC is not an artifact of the culture process. Insulin did not stimulate NOS activity in primary confluent cultured cells because it did not affect citrulline or combined NO(-)(3)/NO(-)(2) production. To see whether insulin required the permissive presence of NO to stimulate cGMP production, iNOS and basal cGMP production were inhibited with L-NMMA, and the cells were incubated with or without 1 nM insulin and/or the NO donor, S-nitroso-N-acetyl-D,L-penicillamine (SNAP) at a concentration (0.1 microM) that restored cGMP production to the basal value. In the presence of L-NMMA, insulin no longer affected cGMP production but when insulin was added to L-NMMA plus SNAP, cGMP production was increased by 69% (P < 0.05 vs. L-NMMA plus SNAP). Insulin, which increases glucose uptake by these cells, increased the cell lactate content and the lactate-to-pyruvate ratio (LPR) by 81 and 97%, respectively (both P < 0.05), indicating that the hormone increased aerobic glycolysis and the redox potential. The effects of insulin on LPR and cGMP production were blocked by removing glucose or by adding 2-deoxyglucose to the incubation media and were duplicated by the reducing substrate, beta-hydroxybutyrate. We conclude that insulin does not acutely affect iNOS activity in these VSMC but it does augment cGMP production induced by the NO already present in the cell while increasing aerobic glycolysis and the cell redox potential.

Aerobiosis↗
PubMed1997

An investigation of lower oesophageal redox potentials in gastro-oesophageal reflux patients and healthy volunteers.

Oesophageal electrical properties are thought to be important in the development of gastro-esophageal reflux. This study simultaneously monitored the intraoesophageal pH and redox potentials in 18 patients with gastro-oesophageal reflux symptoms and 15 asymptomatic controls, for a 24 h period. The pH and redox electrodes were positioned 5 cm proximal to the lower oesophageal sphincter, the position of which had been determined by manometry. Since significantly different behaviour was observed during the day and night, the data were divided into periods of waking and sleeping. Data were analysed for acid reflux (pH < 4) and transients in the redox potential-time curve. Both patients and normal subjects showed negative redox transients which were more frequent and pronounced at night than during the day, and which were uncorrelated with acid reflux. The only parameter which was significantly different between normal and refluxing groups was the amount of nocturnal redox activity, which was lower in refluxing subjects than in normals. Some possible hypotheses for these observations, and the origin of the redox species, are discussed.

Adult↗
PubMed1988

EPR determination of interaction redox potentials in a multiheme cytochrome: cytochrome c3 from Desulfovibrio desulfuricans Norway.

In cytochromes c3 which contain four hemes per molecule, the redox properties of each heme may depend upon the redox state of the others. This effect can be described in terms of interaction redox potentials between the hemes and must be taken into account in the characterization of the redox properties of the molecule. We present here a method of measurement of these interactions based on the EPR study of the redox equilibria of the protein. The microscopic and macroscopic midpoint potentials and the interaction potentials are deduced from the analysis of the redox titration curves of the intensity and the amplitude of the EPR spectrum. This analysis includes a precise simulation of the spectrum of the protein in the oxidized state in order to determine the relative contribution of each heme to the spectral amplitude. Using our method on cytochrome c3 from D. desulfuricans Norway, we found evidence for the existence of weak interaction potentials between the hemes. The three interaction potentials which have been measured are characterized by absolute values lower than 20 mV in contrast with the values larger than 40-50 mV which have been reported for cytochrome c3 from D. gigas. Simulations of the spectra of samples poised at different potentials indicate a structural modification of the heme with the most negative potential during the first step of reduction. The correspondence between the redox sites as characterized by the EPR potentiometric titration and the hemes in the tridimensional structure is discussed.

Binding Sites↗
PubMed1997

Changes in the redox potential and catalase activity of Mn2+ ions during formation of Mn-bicarbonate complexes.

Changes in the redox potentials of Mn2+ ions and Mn-bicarbonate complexes were studied due to their possible participation in the photosynthetic oxidation of water in plant photosystem 2 and in H2O2 decomposition. Electrochemical oxidation of Mn2+ ions was demonstrated by voltammetry on a platinum electrode in 0.1 M LiClO4 solution at a potential of 1.19 V (vs NHE). When NaHCO3 was added, the oxidation peak of Mn2+ ions disappeared. New oxidation peaks appeared at 0.92 V and 0.63 V which corresponded to the oxidation of Mn(HCO3)+ and Mn(HCO3)2, respectively, generated by complex formation between Mn2+ and HCO3- ions. The effect of the Mn(2+)-bicarbonate complex on H2O2 redox decomposition was studied. It was shown that the addition of MnSO4 to the H2O2 solution did not affect the H2O2 oxidation peak height thereby indicating the absence of H2O2 decomposition by Mn2+ ions. At the same time, subsequent addition of NaHCO3 resulted in the disappearance of the oxidation peaks of both H2O2 and Mn2+. As at pH 7 the thermodynamic potential of H2O2 reduction is 1.1 V and the Mn2+ oxidation potential is 1.19 V, the redox reaction between them is hampered. Formation of the Mn(2+)-bicarbonate complex shifted the Mn2+ oxidation potential to 0.63 V, thereby inducing the decomposition of H2O2. It is suggested that the decrease in the Mn2+ oxidation potential resulting from the formation of the bicarbonate complex determines the bicarbonate capability to enhance the Mn2+ ability to donate electrons for PS 2 reaction centres.

Bicarbonates↗
PubMed2000

Monitoring the changes of redox potential, pH and electrical conductivity of the mangrove soils in northern Taiwan.

The redox potential (Eh), pH and electrical conductivity (EC) of the marsh soils of the Chuwei mangrove, located in the estuarine of the Tansui River in northern Taiwan were monitored for two years (from October 1995 to September 1997). The soils of selected pedons were studied, and the soils were classified based on Keys to Soil Taxonomy. The soil pH values tended to be neutral due to the impact of seawater on the mangrove marsh. The amounts of organic carbon found in this study area were much less than those generally encountered in the wetland soils of temperate regions in the world. The base saturation percentages of the soils were almost 100%, the exchangeable Na being particularly predominant. The concentrations of various cations of water in this ecosystem were in the order of Na+ > Mg2+ > K+ = Ca2+, and those of anions of water were in the order of Cl- > SO4(2-) > NO3- > PO4(3-). In spite of seasonal flooding changes, highly reduced states (100 to -200 mV of Eh values) existed throughout the two-year study. The spatial and temporal variations of the Eh values of the surface soil (0-20 cm) were higher than those of the subsoils (20-100 cm). The EC values of the soils from the surface to a depth of 100-cm were generally more than 20 dS/m. The marsh soils of the Chuwei mangrove were, thus, classified as Halic Endoaquents or Halic Fluvaquents.

Anions↗
PubMed1998

Influence of herbicide binding on the redox potential of the quinone acceptor in photosystem II: relevance to photodamage and phytotoxicity.

Here we show that herbicide binding influences the redox potential (Em) of the plastoquinone QA/QA- redox couple in Photosystem II (PSII). Phenolic herbicides lower the Em by approximately 45 mV, while DCMU raises the Em by 50 mV. These shifts are reflected in changes in the peak temperature of thermoluminescence bands arising from the recombination of charge pairs involving QA-. The herbicide-induced changes in the Em of QA/QA- correlate with earlier work showing that phenolic herbicides increase the sensitivity of PSII to light, while DCMU protects against photodamage. This correlation is explained in terms of the following hypothesis which is based on reactions occurring in the bacterial reaction center. The back-reaction pathway for P680+QA- is assumed to be modulated by the free-energy gap between the P680+QA- and the P680+Ph- radical pairs. When this gap is small (i.e., when the Em of QA/QA- is lowered), a true back-reaction is favored in which P680+Ph- is formed, a state which decays forming a significant yield of P680 triplet. This triplet state of chlorophyll reacts with oxygen, forming singlet oxygen, a species likely to be responsible for photodamage. When the free-energy gap is increased (i.e., when the Em of QA/QA- is raised), the yield of the P680+Ph- is diminished and a greater proportion of the P680+QA- radical pair decays by an alternative, less damaging, route. We propose that at least some of the phytotoxic properties of phenolic herbicides may be explained by the fact that they render PSII ultrasensitive to light due to this mechanism.

Diuron↗