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At least 307 records · Page 17Linked to original sources
PubMed2003

Element analysis and biological studies on ten oriental spices using XRF and Ames test.

Ten oriental spices were analyzed for their element composition using X-ray fluorescence (XRF): nutmeg (Myristica fragrans), coriander (Coriandrum sativum), safflower (Carthamus tinctorius), caraway (Carum carvi), Sicilian sumac (Rhus coriaria), aniseed (Anisum vulgare), black pepper (Piper nigrum), cardamom (Elettaria cardamomum), cumin (Cuminum cyminum) and nigella (Nigella sativum). The spices were found to contain the following elements: Mg, Al, Si, P, S, Cl, K, Ca, Ti, Mn, Fe, Cu and Zn, with varying concentrations. Mutagenic studies using Salmonella typhimurium strains TA97a, TA98, TA100, and TA102 showed that the above spices have no base pair substitution mutagenic activity. However, a weak frameshift mutagenicity has been shown by nutmeg and a very weak oxidative mutagenic action has been revealed by cumin.

Asia↗
PubMed1995

Structural and spectroscopic studies of the copper site of stellacyanin.

The structure of the copper site in oxidized and reduced Rhus vernicifera stellacyanin has been studied by X-ray absorption (XAFS) spectroscopy at different pH values. Data for the oxidized protein are consistent with the fourth ligand being an O- or N-donating ligand rather than a cysteine from the disulfide bridge. The fourth ligand is not present in the inner coordination sphere, but makes a more distant interaction 2.7 A from the copper atom. Only minor changes in the details of the Cu(II) coordination occur when the pH is varied. Direct structural information on reduced stellacyanin is provided. Upon reduction, one of the histidine ligands moves away from the copper atom by at least 0.2 A. A low-Z (O or N) scatterer is present approximately 2.4 A from the Cu(I) atom in the protein at low pH, and this ligand is lost at high pH. There is no evidence for an S-donating fourth ligand in the reduced protein. The XAFS results are presented in relation to the spectroscopic and structural information available for some methionine-121 mutants of azurin. The data reveal that there are spectroscopic similarities between stellacyanin and some of the mutant proteins, but distinct structural differences exist that preclude these proteins as suitable models for the copper site of stellacyanin.

Azurin↗
PubMed1992

Kinetics of electron transfer between cytochrome c and laccase.

Rate constants have been determined for the electron-transfer reactions between reduced horse heart cytochrome c and resting Rhus vernicifera laccase as a function of pH, ionic strength, and temperature. The second-order rate constant for the oxidation of reduced cytochrome c was determined to be k = 125 M-1 s-1 at 25 degrees C in 0.2 M phosphate buffer at pH 6.0 with the activation parameters delta H++ = 16.2 kJ mol-1 and delta S++ = 28.9 J mol-1 K-1. The rate constants increased with decreasing buffer concentration, indicating that electron transfer from cytochrome c to laccase is favored by the local electrostatic interaction (ZAZB = -0.9 at pH 6 and -1.3 at pH 4.8) between the basic proteins with positive net charges. From the increase of the rate of electron transfer with decreasing pH, one of the driving forces of the reaction was suggested to be the difference in the redox potentials between the type 1 copper in laccase and the central iron in cytochrome c. Further, on addition of one hexametaphosphate anion per cytochrome c molecule, the rate of the electron transfer was increased, probably because the association of both proteins became more favorable.

Animals↗
PubMed2001

Spectroscopy and reactivity of the type 1 copper site in Fet3p from Saccharomyces cerevisiae: correlation of structure with reactivity in the multicopper oxidases.

Fet3p is a multicopper oxidase recently isolated from the yeast, Saccharomyces cerevisiae. Fet3p is functionally homologous to ceruloplasmin (Cp) in that both are ferroxidases. However, by sequence homology Fet3p is more similar to fungal laccase, and both contain a type 1 Cu site that lacks the axial methionine ligand present in the functional type 1 sites of Cp. To determine the contribution of the electronic structure of the type 1 Cu site of Fet3p to the ferroxidase mechanism, we have examined the absorption, circular dichroism, magnetic circular dichroism, electron paramagnetic resonance, and resonance Raman spectra of wild-type Fet3p and type 1 and type 2 Cu-depleted mutants. The spectroscopic features of the type 1 Cu site of Fet3p are nearly identical to those of fungal laccase, indicating a very similar three-coordinate geometry. We have also examined the reactivity of the type 1 Cu site by means of redox titrations and stopped-flow kinetics. From poised potential redox titrations, the E degrees of the type 1 Cu site is 427 mV, which is low for a three-coordinate type 1 Cu site. The kinetics of reduction of the type 1 Cu sites of four different multicopper oxidases with two different substrates were compared. The type 1 site of a plant laccase (Rhus vernicifera) is reduced moderately slowly by both Fe(II) and a bulky organic substrate, 1,4-hydroquinone (with 6 equiv of substrate, k(obs) = 0.029 and 0.013 s(-)(1), respectively). On the other hand, the type 1 site of a fungal laccase (Coprinus cinereus) is reduced very rapidly by both substrates (k(obs) > 23 s(-)(1)). In contrast, both Fet3p and Cp are rapidly reduced by Fe(II) (k(obs) > 23 s(-)(1)), but only very slowly by 1,4-hydroquinone (10- and 100-fold more slowly than plant laccase, respectively). Semiclassical theory is used to analyze the origin of these differences in reactivity in terms of type 1 Cu site accessibility to specific substrates.

Ceruloplasmin↗
PubMed2002

Novel oxidations of (+)-catechin by horseradish peroxidase and laccase.

Horseradish peroxidase (HRP; EC 1.11.1.7) catalyzed the H(2)O(2)-dependent oxidative coupling of (+)-catechin 1 to form three different biphenyl C-C dimers 2-4, whereas Rhus vernicifera laccase catalyzed the formation of two new catechin-hydroquinone adducts 5 and 6. Spectroscopic evidence showed that HRP dimers were linked through position 8 of the A-ring of one catechin moiety to C-5' of ring B in 2 and 4 and to C-2 of ring C in 3. The unusual catechin dicarboxylic acid dimer 4 was obtained by ortho cleavage of the E-ring. Hydroquinone served as both a shuttle oxidant and a reactant by coupling at C-2' and C-5' of the catechin B-ring during laccase oxidations. HRP and laccase oxidation products were compared to D,L-alpha-tocopherol and (+)-catechin for their abilities to inhibit iron-induced lipid peroxidation in rat brain homogenates and Fe(3+)-ADP/NADPH in rat liver microsomes, as measured by the intensity of thiobarbituric acid reactive substance. All metabolites exhibited anti-lipid peroxidation with IC(50) values approximately 2-8 times higher than those of standard compounds. Characteristic reaction products may prove to be novel markers for (+)-catechin antioxidant reactions in living systems.

Animals↗
PubMed2001

Levels of beta-carotene and effects of processing on selected fruits and vegetables of the arid zone of India.

Some locally available fruits and vegetables of the arid zone of Rajasthan were analyzed for their beta-carotene content; the selected fruits and vegetables were: Dansra (Rhus myserensis), Kachri (Cucumis collosus), fruit Kachri (Cucumis collosus), Kair (Capparis decidua) and Sanghri (Prosopis cineriria). The beta-carotene contents of the samples were estimated in fresh and various processed states (blanched, dried and roasted). The results showed the heat lability of beta-carotene. Among the samples, kair was found to be the richest source of beta-carotene. Variety, too, had an impact on the content of this fat soluble vitamin.

Climate↗
PubMed1988

Cu(I) analysis of blue copper proteins.

A simple colorimetric test for the Cu(I) content in blue copper proteins is described. The procedure is based on the formation of a complex between Cu(I) and 2,2'-biquinoline in an acetic acid medium. Analyses of spinach plastocyanin, Pseudomonas aeruginosa azurin and Rhus vernicifera stellacyanin show that the cysteine residue in the type 1 site does not induce Cu(II) reduction under our conditions. There is evidence in laccase samples for the presence of an endogenous reductant that can reduce 0.14 +/- 0.04 mol of Cu(II)/mol of protein; however, the addition of EDTA eliminates the interference. The analysis shows that 25 +/- 2% of the type 3 copper ions are in the reduced form in the resting enzyme and that 80 +/- 15% of the type 3 copper ions are reduced in preparations of type-2-depleted laccase. There is growing interest in the development of chemically modified forms of laccase, and our method should be very useful for establishing the valence state of the metal centres in the various derivatives.

Azurin↗
PubMed1999

2-Hydroxy-4-methoxybenzaldehyde: a potent tyrosinase inhibitor from African medicinal plants.

By bioassay-guided fractionation using mushroom tyrosinase (EC 1.14.18.1), 2-hydroxy-4-methoxybenzaldehyde was characterized as the principal tyrosinase inhibitor from three East African medicinal plants, the root of Mondia whitei (Hook) Skeels (Asclepiaceae), the root of Rhus vulgaris Meikle (Anacardiaceae), and the bark of Sclerocarya caffra Sond (Anacardiaceae). It inhibited the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) by mushroom tyrosinase with an ID50 of 4.3 micrograms/ml (0.03 mM). The inhibition kinetics analyzed by a Lineweaver-Burk plot found this simple benzaldehyde derivative to be a mixed type inhibitor for this oxidation and affects on the enzyme in several ways. Based on finding this potent tyrosinase inhibitor, various related analogues were also tested in order to gain new insights into their inhibitory functions on a molecular basis.

Animals↗
PubMed1999

Antiviral activities of biflavonoids.

Biflavonoids such as amentoflavone (1), agathisflavone (2), robustaflavone (3), hinokiflavone (4), volkensiflavone (5), rhusflavanone (7), succedaneflavanone (9), all isolated from Rhus succedanea and Garcinia multiflora, as well as their methyl ethers and acetates, volkensiflavone hexamethyl ether (6), rhusflavanone hexaacetate (8), and succedaneflavanone hexaacetate (10) were evaluated for their antiviral activities. The inhibitory activities against a number of viruses including respiratory viruses (influenza A, influenza B, respiratory syncytial, parainfluenza type 3, adenovirus type 5, and measles) and herpes viruses (HSV-1, HSV-2, HCMV, and VZV) were investigated. The results indicated that robustaflavone exhibited strong inhibitory effects against influenza A and influenza B viruses with EC50 values of 2.0 micrograms/ml and 0.2 microgram/ml, respectively, and selectivity index values (SI) of 16 and 454, respectively. Amentoflavone and agathisflavone also demonstrated significant activity against influenza A and B viruses. Amentoflavone and robustaflavone exhibited moderate anti-HSV-1 anti-HSV-2 activities with EC50 values of 17.9 micrograms/ml (HSV-1) and 48.0 micrograms/ml (HSV-2) and SI values of > 5.6 (HSV-1) and > 2.1 (HSV-2) for amentoflavone; EC50 values of 8.6 micrograms/ml (HSV-1) and 8.5 micrograms/ml (HSV-2), and SI values of > 11.6 (HSV-1) and > 11.8 (HSV-2) for robustaflavone. Rhusflavanone demonstrated inhibitory activities against influenza B, measles, and HSV-2 viruses with SI values of 9.3, 8 and > 6.4, respectively. Succedaneaflavanone exhibited inhibitory activities against influenza B virus and VZV with SI values of 15 and < 3.0, respectively.

Antiviral Agents↗
PubMed2001

Black spot poison ivy: A report of 5 cases and a review of the literature.

Black-spot poison ivy dermatitis is a rare manifestation of a common condition. It occurs on exposure to the resins of the plants of the Rhus family also known as Toxicodendron. We describe 5 patients with black deposits on their skin and clothing after contact with poison ivy and review the literature reflecting different aspects of this phenomenon including clinical presentation, histologic findings, and historical background.

Adolescent↗
PubMed1972

Kinetics of the reduction of metalloproteins by chromous ion (laccase-cytochrome c-plastocyanins-temperature-rate constants).

The reduction of Cu(330) in Rhus vernicifera laccase by chromous ion is 30% faster than reduction of Cu(614) at room temperature [pH 4.8, mu = 0.1 (NaCl)], and two parallel first-order paths, attributed to heterogeneity of the protein, are observed at both wavelengths. The reactions of stellacyanin, spinach and French-bean plastocyanins, and cytochrome c with chromous ion under similar conditions are faster than that with laccase by factors of 10(2) to 10(4), and are first order in protein concentration. Comparison of rates and activation parameters for the reduction of "blue" copper in laccase, stellacyanin, and the two plastocyanins indicates that reduction of the Cu(614) site in laccase may occur by intramolecular electron transfer from one of the Cu(330) sites. Our value of DeltaHdouble dagger (17.4 kcal/mol) for the chromous ion reduction of cytochrome c is consistent with a mechanism in which major conformational changes in the protein must accompany electron transfer.

Animals↗
PubMed1976

Spectroscopic studies and a structural model for blue copper centers in proteins.

Low temperature absorption, circular dichroism, and magnetic circular dichroism spectral studies of the blue copper proteins Rhus vernicifera stellacyanin, bean plastocyanin, and Pseudomonas aeruginosa azurin have been made. Low energy bands attributable to the d-d transitions 2B2 leads to 2E and 2B2 leads to 2B1 in a flattened tetrahedral (D 2d) copper-(II) center are observed in these proteins at about 5000 and 10,000 cm-1, respectively. The band positions accord well with ligand field calculations based on a tetrahedral structure that is distorted approximately 6 degrees toward a square plane. The ligands in this flattened tetrahedral coordination unit in bean plastocyanin are identified from various spectroscopic experiments as His-38, Cys-85, His-88, and a deprotonated peptide nitrogen (N) a few residues above His-38.

Azurin↗
PubMed1978

Reductant-dependent electron distribution among redox sites of laccase.

Rhus laccase (monophenol monooxygenase, monophenol,dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1) an O2/H2O oxidoreductase containing four copper ions bound to three redox sites (type 1, type 2, and type 3 Cu pair), was titrated anaerobically with several reductants having various chemical and thermodynamic properties. The distribution of electron equivalents among the redox sites was found to be reductant dependent. When the data for titration by various reductants of the type 3 site were plotted against those of the type 1 site according to the Nernst formalism, the slope n varied from 2.0 to 1.0. The redox potential of the reductant's first oxidation step is qualitatively correlated with the value of n and is suggested as the factor that modulates the electron distribution. Such a behavior implies a nonequilibrium situation. A very good simulation of the data was provided by an analysis assuming a formally variable cooperativity between the two type 3 copper ions. This apparent variability is suggested to result from a process whereby sufficiently strong reductants induce a transition of the type 3 site from a cooperative two-electron acceptor to a pair of independent one-electron acceptors. This uncoupled state of the type 3 site is considered metastable. Other possible models were also investigated. Summarizing the available data, we conclude that the two-electron accepting behavior of the 330-nm chromophore is the exception rather than the rule.

Anaerobiosis↗
PubMed1978

Magnetic susceptibility studies of laccase and oxyhemocyanin.

The magnetic susceptibility of Rhus vernicifera laccase has been remeasured over the temperature range 5-260 K. In contrast to our previous results [Solomon, E.I., Dooley, D. M., Wang R.-H., Gray, H.B., Cerdonio, M., Mogno, F. & Romani, G. L. (1975) J. Am. Chem. Soc. 98, 1029-1031] linear chi versus T-1 behavior was observed. The susceptibility of Limulus polyphemus oxyhemocyanin has also been measured in the range 5-260 K. Only weak paramagnetism, attributable to dissolved oxygen and a small amount of paramagnetic impurities, was observed. Analysis of the data establishes a lower limit of 550 cm-1 for J, consistent with our earlier work. The temperature dependence of the susceptibility of laccase is quantitatively accounted for by the presence of two paramagnetic copper ions (types 1 and 2) per enzyme molecule. Curie law behavior at low temperatures rules out significant interaction between the two coppper types, indicating that these redox centers are well separated (several angstroms) and are not connected by bridging ligands. Formulation of the type 3 site as binuclear Cu(II) requires J greater than or equal to 500 cm-1.

Animals↗
PubMed1997

Retrobiosynthetic NMR studies with 13C-labeled glucose. Formation of gallic acid in plants and fungi.

The biosynthesis of gallic acid was studied in cultures of the fungus Phycomyces blakesleeanus and in leaves of the tree Rhus typhina. Fungal cultures were grown with [1-13C]glucose or with a mixture of unlabeled glucose and [U-13C6]glucose. Young leaves of R. typhina were kept in an incubation chamber and were supplied with a solution containing a mixture of unlabeled glucose and [U-13C6]glucose via the leaf stem. Isotope distributions in isolated gallic acid and aromatic amino acids were analyzed by one-dimensional 1H and 13C NMR spectroscopy. A quantitative analysis of the complex isotopomer composition of metabolites was obtained by deconvolution of the 13C13C coupling multiplets using numerical simulation methods. This approach required the accurate analysis of heavy isotope chemical shift effects in a variety of different isotopomers and the analysis of long range 13C13C coupling constants. The resulting isotopomer patterns were interpreted using a retrobiosynthetic approach based on a comparison between the isotopomer patterns of gallic acid and tyrosine. The data show that both in the fungus and in the plant all carbon atoms of gallic acid are biosynthetically equivalent to carbon atoms of shikimate. Notably, the carboxylic group of gallic acid is derived from the carboxylic group of an early intermediate of the shikimate pathway and not from the side chain of phenylalanine or tyrosine. It follows that the committed precursor of gallic acid is an intermediate of the shikimate pathway prior to prephenate or arogenate, most probably 5-dehydroshikimate. A formation of gallic acid via phenylalanine, the lignin precursor, caffeic acid, or 3,4, 5-trihydroxycinnamic acid can be ruled out as major pathways in the fungus and in young leaves of R. typhina. The incorporation of uniformly 13C-labeled glucose followed by quantitative NMR analysis of isotopomer patterns is suggested as a general method for biosynthetic studies. As shown by the plant experiment, this approach is also applicable to systems with low incorporation rates.

Carbon Isotopes↗
PubMed1990

Acute allergic contact dermatitis. How to manage severe cases.

An understanding of the causes and course of acute allergic contact dermatitis aids in recognition of this common problem. The most frequent cause is the Rhus group (poison ivy, oak, and sumac), and a large percentage of the US population is sensitized to this group of allergens. With severe cases, prompt administration of systemic corticosteroids alleviates discomfort and shortens the course of disease. Local treatment may give added relief. However, no treatment is as satisfactory as avoidance of contact.

Acute Disease↗
PubMed1978

Carcinogenicity of some folk medicinal herbs in rats.

Twelve medicinal herbs were bioassayed to correlate a high incidence of esophageal carcinoma in natives of different places with their habitual consumption of these products. Outbred NIH Black rats were given 72 weekly sc injections of the total aqueous extracts of the plant materials. The tanninrich plant extracts from Areca catechu and Rhus copallina produced local tumors in 100 and 33%, respectively, of the experimental animals. Other materials included Diospyros virginiana and extracts from plants not rich in tannins. Diospyros and extracts of Sassafras albidum and Chenopodium ambrosiodes were tumorigenic in over 50% of the treated animals.

Animals↗
PubMed1992

Laccase from Sycamore Maple (Acer pseudoplatanus) Polymerizes Monolignols.

Current understanding of the final oxidative steps leading to lignin deposition in trees and other higher plants is limited with respect to what enzymes are involved, where they are localized, how they are transported, and what factors regulate them. With the use of cell suspension cultures of sycamore maple (Acer pseudoplatanus), an in-depth study of laccase, one of the oxidative enzymes possibly responsible for catalyzing the dehydrogenative polymerization of monolignols in the extracellular matrix, was undertaken. The time course for secretion of laccase into suspension culture medium was determined with respect to age and mass of the cells. Laccase was completely separated from peroxidase activity by hydrophobic interaction column chromatography, and its purity was assessed with different types of gel electrophoresis (isoelectric focusing-, native-, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis). Amino acid and glycosyl analyses of the purified enzyme were compared with those reported from previous studies of plant and fungal laccases. The specific activity of laccase toward several common substrates, including monolignols, was determined. Unlike a laccase purified from the Japanese lacquer tree (Rhus vernicifera), laccase from sycamore maple oxidized sinapyl, coniferyl, and p-coumaryl alcohols to form water-insoluble polymers (dehydrogenation polymers).

Journal Article↗