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PubMed2004

Flavoprotein disulfide reductases: advances in chemistry and function.

The flavoprotein disulfide reductases represent a family of enzymes that show high sequence and structural homology. They catalyze the pyridine-nucleotide-dependent reduction of a variety of substrates, including disulfide-bonded substrates (lipoamide dehydrogenase, glutathione reductase and functional homologues, thioredoxin reductase, and alkylhydroperoxide reductase), mercuric ion (mercuric ion reductase), hydrogen peroxide (NADH peroxidase), molecular oxygen (NADH oxidase), and the reductive cleavage of a carbonyl-activated carbon-sulfur bond followed by carboxylation (2-ketopropyl-coenzyme-M carboxylase?oxidoreductase). They use at least one nonflavin redox center to transfer electrons from reduced pyridine nucleotide to their substrate through flavin adenine dinucleotide. The nature of the nonflavin redox center located adjacent to the flavin varies and three types have been identified: an enzymic disulfide (most commonly), an enzymic cysteine sulfenic acid (NADH peroxidase and NADH oxidase), and a mixed Cys-S-S-CoA disulfide (coenzyme A disulfide reductase). Selection of the particular nonflavin redox center and utilization of a second, or even a third, nonflavin redox center in some cases presumably represents the most efficient strategy for reduction of the individual substrate.

Disulfides↗
PubMed1993

Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation.

Sulfenic acids (R-SOH) result from the stoichiometric oxidations of thiols with mild oxidants such as H2O2; in solution, however, these derivatives accumulate only transiently due to rapid self-condensation reactions, further oxidations to the sulfinic and/or sulfonic acids, and reactions with nucleophiles such as R-SH. In contrast, oxidations of cysteinyl side chains in proteins, where disulfide bond formation can be prevented and where the reactivity of the nascent cysteine-sulfenic acid (Cys-SOH) can be controlled, have previously been shown to yield stable active-site Cys-SOH derivatives of papain and glyceraldehyde-3-phosphate dehydrogenase. More recently, however, functional Cys-SOH residues have been identified in the native oxidized forms of the FAD-containing NADH peroxidase and NADH oxidase from Streptococcus faecalis; these two proteins constitute a new class within the flavoprotein disulfide reductase family. In addition, Cys-SOH derivatives have been suggested to play important roles in redox regulation of the DNA-binding activities of transcription factors such as Fos and Jun, OxyR, and bovine papillomavirus type 1 E2 protein. Structural inferences for the stabilization of protein-sulfenic acids, drawn from the refined 2.16-A structure of the streptococcal NADH peroxidase, provide a molecular basis for understanding the proposed redox functions of these novel cofactors in both enzyme catalysis and transcriptional regulation.

Catalysis↗
PubMed1980

Theoretical and experimental study of an immobilized bienzyme system. Computer calculations and electron microscopy visualization of local concentration profiles.

A cytochemical method was used in order to visualize the existence of local concentrations of metabolites within an immobilized bienzyme system. Glucose oxidase (EC 1.1.3.4) and peroxidase (EC 1.11.1.7) were immobilized together into an artificial proteic membrane obtained by a previously described co-cross-linking process using a bifunctional agent, glutaraldehyde. The cytochemical reagent 3,3'-diaminobenzidine was used as a hydrogen donor substrate and kinetic studies were performed with both free and immobilized forms of the enzymes; in the latter case, a new direct method was introduced which allowed kinetic studies on the visualization system itself. From experimental kinetic parameters, theoretical concentrations profiles were calculated by computer using numerical analysis methods. These results were discussed with special attention to the electron microscopic observations. Computer simulations were in good agreement with electron micrographs. No geometrical similarity was seen in our system between poly(3,3'-diaminobenzidine) precipitate distribution and peroxidase molecule homogeneous location.

Computers↗
PubMed2004

Ultrastructural localization of thyroid peroxidase, hydrogen peroxide-generating sites, and monoamine oxidase in benign and malignant thyroid diseases.

Despite thyroid tissue heterogeneity, biochemical and morphological features have been associated with certain thyroid diseases. We analyzed the ultracytochemical localization of thyroperoxidase (TPO), TPO-associated hydrogen peroxide-generating sites (H(2)O(2) sites), and monoamine oxidase (MAO) in terms of morphology and biochemical TPO activity in abnormal thyroids. We examined 11 cases of nontoxic multinodular goiter, 5 cases of Hashimoto's thyroiditis, 1 case of oncocytic (Hürthle or oxyphilic cell) adenoma, 5 cases of Graves' disease, 4 cases of papillary carcinoma, and 4 cases of perinodular normal tissue. In the perinodular tissue, TPO was detected mainly in the nuclear envelope, rough endoplasmic reticulum (RER), and subapical vesicles, but not in the apical surface. In multinodular goiter, heterogeneous TPO reactivity ranging from almost null to strongly positive was detected in similar locations as in the perinodular tissue, and was absent in the microvilli. Follicular cells from Hashimoto's thyroiditis displayed TPO in the nuclear envelope and the scarce RER. Remarkably, oncocytic cells from both Hashimoto's thyroiditis and oncocytic adenoma, typically packed with mitochondria, displayed evident TPO reaction exclusively in mitochondrial cristae. In Graves' disease, the nuclear envelope, enlarged RER, and apical vesicles were strongly TPO positive, and microvilli also exhibited TPO activity. Papillary carcinoma cells were negative for TPO. The localization and characteristics of TPO activity in the H(2)O(2) sites were similar to that of TPO in all tissues. MAO was positive in mitochondria of perinodular tissues, multinodular goiter, and oncocytes and negative in Hashimoto's thyroiditis and Graves' disease. Interestingly, MAO was intensely positive in the nuclear envelope of papillary carcinoma but unreactive in mitochondria. Biochemical TPO activity was increased in multinodular goiter and Graves' disease. In conclusion, several changes in ultracytochemical characteristics of TPO, H(2)O(2) sites, and MAO were associated with thyroid disease. Nonmalignant oncocytic cells exhibited an unusual mitochondrial location of TPO and H(2)O(2) sites. The distribution of MAO in nuclear envelope of papillary carcinoma cells could be a further feature of malignancy.

Humans↗
PubMed1977

Cross-linking of protein by peroxidase.

The reaction products of peroxidase, a hydrogen donor and hydrogen peroxide decreased the amount of lysine recovered from proteins after acid hydrolysis. Oxidation of peroxidase treated proteins with performic acid prior to hydrolysis formed alpha-amino adipic acid indicating that the peroxidase or the quinones formed by peroxidase had oxidatively deaminated some lysyl residues of the protein to form lysyl aldehyde. Gel filtration and polyacrylamide gel electrophoresis revealed dimers, trimers and higher protein polymers that were not detected when peroxidase was omitted. Since some of the protein polymers were not dissociated by gel electrophoresis in the presence of dodecyl sulfate, urea and mercaptoethanol, it suggests that the free radicals or quinones formed by peroxidase had interacted with or cross-linked protein molecules by the formation of covalent bonds. Oxidative enzymes like peroxidase and polyphenol oxidase may lower the nutritive value of proteins by the oxidative deamination of lysine, reaction with cysteine and methionine and by cross-linking protein molecules to reduce their susceptibility to enzymatic hydrolysis.

2-Aminoadipic Acid↗
PubMed1999

Oxygen metabolism by Treponema denticola.

Treponema denticola strains ATCC 35405 and ASLM were found to have moderately active oxygen metabolism and consumed some 0.46 mumol O2/h/mg cell protein in anaerobic growth medium or about ten times this amount in aerobic medium. There appeared to be no differences between the two strains in their oxidative metabolism. The spirochetes showed significant endogenous O2 utilization, which was stimulated only slightly by added glucose or arginine, moderately by glycine, but markedly by casamino acids or brain-heart infusion broth. O2 metabolism by intact cells was insensitive to cyanide and so did not appear to involve cyanide-sensitive cytochrome oxidases. Moreover, difference spectra of cell extracts and membranes did not reveal heme profiles. However, the spirochetes did have very active reduced nicotinamide adenine dinucleotide (NADH) oxidase(s) and also contained the protective enzymes NADH peroxidase and superoxide dismutase. Both the oxidase(s) and the peroxidase had rather broad substrate specificities. Either NADH or reduced nicotinamide adenine dinucleotide phosphate could serve as reductant, and the enzymes were active with a variety of oxidants. Enzyme activity in fresh cell extracts was only somewhat stimulated by added flavins, but after frozen storage, the activity became much more activated by flavin adenine nucleotide, and to a lesser extent, by flavin mononucleotide. The enzymes were insensitive to fluoride, which inhibits heme-based but not flavin-based oxidases at low pH values. Clearly, these anaerobic spirochetes have significant oxygen metabolism, even at the low levels of O2 measured in periodontal pockets and contain enzymes that offer at least moderate protection against damage by reactive oxygen species.

Anaerobiosis↗
PubMed1999

Ascorbic acid metabolism in pea seedlings. A comparison of D-glucosone, L-sorbosone, and L-galactono-1,4-lactone as ascorbate precursors

L-Ascorbic acid (AsA) accumulates in pea (Pisum sativum L.) seedlings during germination, with the most rapid phase of accumulation coinciding with radicle emergence. Monodehydroascorbate reductase and dehydroascorbic acid reductase were active in the embryonic axes before AsA accumulation started, whereas AsA oxidase and AsA peroxidase activities increased in parallel with AsA. Excised embryonic axes were used to investigate the osone pathway of AsA biosynthesis, in which D-glucosone and L-sorbosone are the proposed intermediates. [U-14C]Glucosone was incorporated into AsA and inhibited the incorporation of [U-14C]glucose (Glc) into AsA. A higher D-glucosone concentration (5 mM) inhibited AsA accumulation. L-Sorbosone did not affect AsA pool size but caused a small inhibition in the incorporation of [U-14C]Glc into AsA. Oxidase and dehydrogenase activities capable of converting Glc or Glc-6-phosphate to glucosone were not detected in embryonic axis extracts. The osones are therefore unlikely to be physiological intermediates of AsA biosynthesis. L-Galactono-1,4-lactone, recently proposed as the AsA precursor (G.L. Wheeler, M.A. Jones, N. Smirnoff [1998] Nature 393: 365-369), was readily converted to AsA by pea embryonic axes. Although L-galactono-1,4-lactone did not inhibit [14C]Glc incorporation into AsA, this does not mean that it is not a precursor, because competition between endogenous and exogenous pools was minimized by its very small pool size and rapid metabolism.

Journal Article↗
PubMed2002

Lignin degrading system of white-rot fungi and its exploitation for dye decolorization.

With global attention and research now focused on looking for the abatement of pollution, white-rot fungi is one of the hopes of the future. The lignin-degrading ability of these fungi have been the focus of attention for many years and have been exploited for a wide array of human benefits. This review highlights the various enzymes produced by white-rot fungi for lignin degradation, namely laccases, peroxidases, aryl alcohol oxidase, glyoxal oxidase, and pyranose oxidase. Also discussed are the various radicals and low molecular weight compounds that are being produced by white-rot fungi and its role in lignin degradation. A brief summary on the developments in research of decolorization of dyes using white-rot fungi has been made.

Coloring Agents↗
PubMed1995

Involvement of an extracellular H2O2-dependent ligninolytic activity of the white rot fungus Pleurotus ostreatus in the decolorization of Remazol brilliant blue R.

During solid-state fermentation of wheat straw, a natural lignocellulosic substrate, the white rot fungus Pleurotus ostreatus produced an extracellular H2O2-requiring Remazol brilliant blue R (RBBR)-decolorizing enzymatic activity along with manganese peroxidase, manganese-independent peroxidase, and phenol oxidase activities. The presence of RBBR was not essential for the production of RBBR-decolorizing enzymatic activity by P. ostreatus, because this activity was also produced in the absence of RBBR. This RBBR-decolorizing enzymatic activity in crude enzyme preparations of 14- and 20-day-old cultures exhibited an apparent Km for RBBR of 31 and 52 microM, respectively. The RBBR-decolorizing enzyme activity was maximal in the pH range 3.5 to 4.0. This activity was independent of manganese, and veratryl alcohol had no influence on it. Manganese peroxidase of P. ostreatus did not decolorize RBBR. This H2O2-dependent RBBR-decolorizing enzymatic activity behaved like an oxygenase possessing a catalytic metal center, perhaps heme, because it was inhibited by Na2S2O5, NaCN, NaN3, and depletion of dissolved oxygen. Na2S2O5 brought an early end to the reaction without interfering with the initial reaction rate of RBBR oxygenase. The activity was also inhibited by cysteine. Concentrations of H2O2 higher than 154 microM were observed to be inhibitory as well. Decolorization of RBBR by P. ostreatus is an oxidative process.

Anthraquinones↗
PubMed1994

[Studies on the effects of low-dose selenium and high-dose cadmium on myocardial injury].

The effects of low-dose selenium and high-dose cadmium on myocardial injury were studied in weanling S.D. rats fed with feed containing controlled levels of selenium and cadmium. Results indicated low-dose selenium and high-dose cadmium could injure heart and myocardial cell membrane system to a certain extent, and cause focal necrosis and reduction in activities of glutathione peroxidase and cytochrome oxidase of heart muscle in rats. It suggested there were certain factors in the grain produced in the areas where Keshan disease was prevalent, which injured heart muscle in rats. So, selenium supplement could prevent from myocardial injury caused by the grain grown in those areas.

Animals↗
PubMed1997

Activation of arylamines to mutagenic product(s) by two in vitro plant systems.

Plant activation of three isomers of phenylenediamine o- m- and p-phenylenediamine, has been studied. Two in vitro plant systems have been used: Persea americana S117 with mixed-function oxidase (MFO) and peroxidase activities, and Zea mays S9 which contains only peroxidase activity. As genetic endpoint, the classical Salmonella tester strains. TA98 and TA100, their derivatives with high O-acetyltransferase levels (YG1024 and YG1029, respectively) and TA98/1.8-DNP6, deficient in this enzyme, have been assayed. Of the three isomers studied, only m-PDA was activated to mutagenic product(s) by both plant systems. This activation required the bacterial O-acetyltransferase activity to give frameshift mutagenic product(s), detected in TA98 and YG1024 strains. In all the assays the P americana system was more potent than the Z. mays system in activating m-PDA. A slight increase of the number of YG1029 revertants was detected when m-PDA was activated by P. americana, suggesting that this compound can be also converted into ultimate mutagenic product(s) that induce base-pair substitutions. m-PDA activation by Z. mays was dependent on the peroxidase activity of this system, but the activation produced by P. americana was totally dependent on MFOs, because a total inhibition of the mutagenic response was found when these activities were inhibited. In addition, the P. americana system was more potent in generating proximal mutagenic forms from m-PDA than S9 from non-induced rat liver, although S9 from Aroclor 1254-induced Sprague-Dawley male rats was the most potent system in the m-PDA activation. These results indicate that the P. americana system can be useful in determining the role of mixed-function oxidases in plant activation of xenobiotics.

Animals↗
PubMed2004

Degradation of juglone by Pleurotus sajor-caju.

The toxic naphthoquinone juglone (5-hydroxy-1,4-naphthoquinone) is efficiently degraded by the ligninolytic fungus Pleurotus sajor-caju, as demonstrated by the total bleaching within 9 d of a conventional liquid culture medium supplemented with 0.6 mM juglone. The oxidative degradation involves the production of hydrogen peroxide arising from both enzymic and non-enzymic oxidation reactions, promoted by the fungus. Juglone is not directly attacked by the oxidative enzymes of the ligninolytic machinery of P. sajor-caju, such as laccase, manganese peroxidase and arylalcohol oxidase. On the other hand, this naphthoquinone is a good substrate for a reductase, which triggers an auto-oxidative process producing reactive oxygen species and leading to juglone degradation. The degradation process continues to completion by means of a direct, presumably non-catalysed reaction with hydrogen peroxide.

Alcohol Oxidoreductases↗
PubMed2004

Screening of laccase, manganese peroxidase, and versatile peroxidase activities of the genus Pleurotus in media with some raw plant materials as carbon sources.

Species of the genus Pleurotus are among the most efficient natural species in lignin degradation belonging to the subclass of ligninolytic organisms that produce laccase (Lac), Mn-dependent peroxidase (MnP), versatile peroxidase (VP), and the H2O2-generating enzyme aryl-alcohol oxidase, but not lignin peroxidases. Production of Lac and oxidation of 2,6-dimethoxyphenol (DMP) in the presence and absence of Mn2+ were detected both in submerged fermentation (SF) of dry ground mandarine peels and in solid-state fermentation (SSF) of grapevine sawdust in all investigated Pleurotus species and strains. Evidence of cultivation methods having a distinct influence on the level of enzyme activities has been demonstrated. Most of the species and strains had higher Lac activity under SSF conditions than under SF conditions. DMP oxidation in the presence and absence of Mn2+ was detected in all investigated species and strains, but was lower under SF conditions than under SSF conditions for most of them. However, relative activities of DMP oxidation in the absence of Mn2+, as percentages of activity against DMP in the presence of Mn2+, were higher under conditions of SF than in SSF cultures in most of the investigated species and strains. The obtained results showed that strains of different origins have different efficiently ligninolytic systems and that conditions of SSF are more favorable for ligninolytic activity than those in SF owing to their similarity to natural conditions on wood substrates.

Carbon↗
PubMed1999

Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides.

An unusual flavoprotein disulfide reductase, which catalyzes the NADPH-dependent reduction of CoASSCoA, has recently been purified from the human pathogen Staphylococcus aureus [delCardayré, S. B., Stock, K. P., Newton, G. L., Fahey, R. C., and Davies, J. E. (1998) J. Biol. Chem. 273, 5744-5751]. Coenzyme A-disulfide reductase (CoADR) lacks the redox-active protein disulfide characteristic of the disulfide reductases; instead, NADPH reduction yields 1 protein-SH and 1 CoASH. Furthermore, the CoADR sequence reveals the presence of a single putative active-site Cys (Cys43) within an SFXXC motif also seen in the Enterococcus faecalis NADH oxidase and NADH peroxidase, which use a single redox-active cysteine-sulfenic acid in catalysis. In this report, we provide a detailed examination of the equilibrium properties of both wild-type and C43S CoADRs, focusing on the role of Cys43 in the catalytic redox cycle, the behavior of both enzyme forms on reduction with dithionite and NADPH, and the interaction of NADP+ with the corresponding reduced enzyme species. The results of these analyses, combined with electrospray mass spectrometric data for the two oxidized enzyme forms, fully support the catalytic redox role proposed for Cys43 and confirm that this is the attachment site for bound CoASH. In addition, we provide evidence indicating dramatic thermodynamic inequivalence between the two active sites per dimer, similar to that documented for the related enzymes mercuric reductase and NADH oxidase; only 1 FAD is reduced with NADPH in wild-type CoADR. The EH2.NADPH/EH4.NADP+ complex which results is reoxidized quantitatively in titrations with CoASSCoA, supporting a possible role for the asymmetric reduced dimer in catalysis.

Catalysis↗
PubMed1993

Miniaturized flexible amperometric lactate probe.

A flexible lactate electrode was made of 400 +/- 100 7-micron-diameter carbon fibers, epoxy embedded in a 0.3-mm-diameter polyimide tubing. The electrode was modified by precipitating on it the relatively insoluble complex formed between 1100 kDa partially N-ethylamine quaternized poly[(vinylpyridine)-Os(bipyridine)2Cl]Cl (POs-EA) and lactate oxidase. The steady-state lactate electrooxidation current, at 2 mM lactate concentration and at 22 degrees C, was 400 nA. The 50 +/- 10 microAc cm-2 current density and the 20 mA cm-2 M-1 sensitivity decreased only by 5% when the partial pressure of oxygen was increased from 0.0 to 0.2 atm. The electrode retains its sensitivity after dry storage at 4 degrees C for 4 months in air but loses half of its sensitivity in 7 h at 37 degrees C through polymer desorption when operated at 0.4 V (SCE). To eliminate interference by species that are electrooxidized at 0.4 V (SCE), the lactate-sensing probe was (a) electrically insulated with an epoxy made of poly(vinylimidazole) cross-linked with ethylene glycol diglycidyl ether and (b) coated with an immobilized horseradish peroxidase (HRP)/glucose oxidase (GOX) film. The latter film was formed by coimmobilizing the two enzymes through periodate oxidation of their oligosaccharides to aldehydes and forming Schiff bases between the polyaldehydes and the enzymes' lysyl amines. In the presence of 1 mM glucose and in air, the interfering electrooxidation of 0.1 mM ascorbate was reduced by a factor of 20. This reduction results from formation of hydrogen peroxide in the glucose-catalyzed reaction and H2O2 oxidation of the ascorbate in a reaction catalyzed by HRP.

Biosensing Techniques↗
PubMed1993

Amperometric sensors for peroxide, choline, and acetylcholine based on electron transfer between horseradish peroxidase and a redox polymer.

Amperometric sensors have been developed for hydrogen peroxide, choline, and acetylcholine by immobilization of horseradish peroxidase, (HRP), choline oxidase, and acetylcholinesterase in a cross-linked redox polymer deposited on glassy carbon electrodes. Peroxide sensors, prepared by immobilization of HRP alone, gave detection limits of 10 nM and a linear response up to ca. 1 mM. Coimmobilization of HRP and glucose oxidase was used to establish the feasibility of highly efficient bienzyme sensors at low substrate levels. Replacing glucose oxidase with choline oxidase produced sensors with submicromolar detection limits and a linear response up to 0.8 mM. Addition of acetylcholinesterase to the sensors generated a relatively small response to acetylcholine that demonstrates the feasibility of trienzyme sensors. At low substrate concentrations, no loss in sensitivity during a 1-day experiment was observed. The response times of these sensors are all less than 30 s with 2-s response times achieved in some cases.

Acetylcholine↗
PubMed1990

The role of endogenous free radical scavengers on tissue recovery in the experimental ulcer model.

The role of lipid peroxidation and endogenous oxygen-derived free radical scavengers on ischemia-reperfusion injury and tissue recovery in rat ulcer model corresponding to the gastric histopathology was investigated. Male Wistar rats weighting 200-250 g were heparinized before occlusion of the celiac axis for 1.5 h. Endogenous CuZn-superoxide dismutase (SOD), Mn-SOD, glutathione peroxidase, fumarase, cytochrome c oxidase, and thiobarbituric acid-reactive compounds as lipid peroxidation products were measured in the gastric tissue at 3 h, and 1, 2, 4, and 7 days after release and in the controls (no occlusion). At 3 h after release, erosion of the gastric mucosa was observed, and gastric ulcers beyond the muscularis mucosae were present in the gastric body 2 days later. Seven days after release, gastric ulcers had disappeared. Activity levels for all five enzymes (CuZn-SOD, Mn-SOD, glutathione peroxidase, fumarase, and cytochrome c oxidase) were low for days 1-4 after release and did not return to control levels by the seventh day. It was observed that the ulcer formation, as evidenced by the histopathology, was significantly related to the levels of endogenous CuZn-SOD, Mn-SOD, glutathione peroxidase, fumarase, and cytochrome c oxidase activities. Thiobarbituric acid-reactive compounds were also low through the entire course of ulcer formation. The study concludes that decreases in the levels of these oxygen-derived free radical scavengers may result in the formation of gastric ulcers; however, endogenous free-radical scavengers may not correspond with tissue recovery. Lipid peroxidation may not be related to ulcer formation.

Animals↗