Selective oxidation of 5-hydroxymethylfurfural using monometallic and bimetallic supported nanoparticles

This work deals with the oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-furandicarboxylic acid (FDCA) using metal supported catalysts. Catalysts were prepared from the immobilisation of preformed monometallic (Au, Pd) and bimetallic (AuCu, AuPd) nanoparticles on commercial oxides (TiO2, CeO2). Au-TiO2 catalyst was found to be very active for HMF oxidation; however, this system deactivated very fast. For this reason, we prepared bimetallic gold-copper nanoparticles and an increase in the catalytic activity was observed together with an increase in catalyst stability. In order to optimise the interaction of the metal active phase with the support, Au and AuCu nanoparticles were supported onto CeO2. Au-CeO2 catalyst was found to be more active than the bimetallic one, leading to the conclusion that in this case the most important feature is the interaction between gold and the support. Catalyst pre-treatments (calcination and washing) were carried out to maximise the contact between the metal and the oxide and an increase in the FDCA production could be observed. The presence of ceria defective sites was crucial for FDCA formation. Mesoporous cerium oxide was synthesised with the hard template method and was used as support for Au nanoparticles to promote the catalytic activity. In order to study the role of active phase in HMF oxidation, PdAu nanoparticles were supported onto TiO2. Au and Pd monometallic catalysts were very active in the formation of HMFCA (5-hydroxymethyl-2-furan carboxylic acid), but Pd was not able to convert it, leading to a low FDCA yield. The calcination of PdAu catalysts led to Pd segregation on the particles surface, which changed the reaction pathway and included an important contribution of the Cannizzaro reaction. PVP protected PdAu nanoparticles, synthesised with different morphologies (core-shell and alloyed structure), confirmed the presence of a different reaction mechanism when the metal surface composition changes.

Selective photo-oxidation of glucose

Biomass transformation into high-value chemicals has attracted attention according to the “green chemistry” principles. Low price and high availability make biomass one of the most interesting renewable resources as it provides the means to create sustainable alternatives to the oil-derived building blocks of the chemical industry In recent year, the need for alternative environmentally friendly routes to drive chemical reactions has in photocatalytic processes an interesting way to obtain valuable chemicals from various sources using the solar light as energy source. The purpose of this work was to use supported noble metal nanoparticles in the selective photo-oxidation of glucose through using visible light. Glucose was chosen as model molecule because it is the cheapest and the most common monosaccharide. Few studies about glucose photo oxidation have been conducted so far, and reaction mechanism is still not totally explained. The aim of this work was to systematically analyze and assess the impact of several parameters (eg. catalyst/substrate ratio, reaction time, effect of the solvent and light source) on the reaction pathway and to monitor the product distribution in order to draw a general reaction scheme for the photo oxidation of glucose under visible light. This study regards the reaction mechanism and the influence of several parameters, such as solvent, light power and substrate concentration. Furthermore, the work focuses on the influence of gold and silver nanoparticles and on the influence of metal loading. The glucose oxidation was monitored through the mass balance and the products selectivity. Reactions were evaluated in terms of glucose conversion, mass balance and selectivities towards arabinose and gluconic acid. In conclusion, this study is able to demonstrate that the photo oxidation of glucose under visible light is feasible; the full identification of the main products allows, for the first time, a comprehensive reaction mechanism scheme.

The sensitivity of the photostationary state of NOx and its implication for the oxidation capacity in a semi-rural and boreal forest region

Für das Vermögen der Atmosphäre sich selbst zu reinigen spielen Stickstoffmonoxid (NO) und Stickstoffdioxid (NO2) eine bedeutende Rolle. Diese Spurengase bestimmen die photochemische Produktion von Ozon (O3) und beeinflussen das Vorkommen von Hydroxyl- (OH) und Nitrat-Radikalen (NO3). Wenn tagsüber ausreichend Solarstrahlung und Ozon vorherrschen, stehen NO und NO2 in einem schnellen photochemischen Gleichgewicht, dem „Photostationären Gleichgewichtszustand“ (engl.: photostationary state). Die Summe von NO und NO2 wird deshalb als NOx zusammengefasst. Vorhergehende Studien zum photostationären Gleichgewichtszustand von NOx umfassen Messungen an unterschiedlichsten Orten, angefangen bei Städten (geprägt von starken Luftverschmutzungen), bis hin zu abgeschiedenen Regionen (geprägt von geringeren Luftverschmutzungen). Während der photochemische Kreislauf von NO und NO2 unter Bedingungen erhöhter NOx-Konzentrationen grundlegend verstanden ist, gibt es in ländlicheren und entlegenen Regionen, welche geprägt sind von niedrigeren NOx-Konzetrationen, signifikante Lücken im Verständnis der zugrundeliegenden Zyklierungsprozesse. Diese Lücken könnten durch messtechnische NO2-Interferenzen bedingt sein - insbesondere bei indirekten Nachweismethoden, welche von Artefakten beeinflusst sein können. Bei sehr niedrigen NOx-Konzentrationen und wenn messtechnische NO2-Interferenzen ausgeschlossen werden können, wird häufig geschlussfolgert, dass diese Verständnislücken mit der Existenz eines „unbekannten Oxidationsmittels“ (engl.: unknown oxidant) verknüpft ist. Im Rahmen dieser Arbeit wird der photostationäre Gleichgewichtszustand von NOx analysiert, mit dem Ziel die potenzielle Existenz bislang unbekannter Prozesse zu untersuchen. Ein Gasanalysator für die direkte Messung von atmosphärischem NO¬2 mittels laserinduzierter Fluoreszenzmesstechnik (engl. LIF – laser induced fluorescence), GANDALF, wurde neu entwickelt und während der Messkampagne PARADE 2011 erstmals für Feldmessungen eingesetzt. Die Messungen im Rahmen von PARADE wurden im Sommer 2011 in einem ländlich geprägten Gebiet in Deutschland durchgeführt. Umfangreiche NO2-Messungen unter Verwendung unterschiedlicher Messtechniken (DOAS, CLD und CRD) ermöglichten einen ausführlichen und erfolgreichen Vergleich von GANDALF mit den übrigen NO2-Messtechniken. Weitere relevante Spurengase und meteorologische Parameter wurden gemessen, um den photostationären Zustand von NOx, basierend auf den NO2-Messungen mit GANDALF in dieser Umgebung zu untersuchen. Während PARADE wurden moderate NOx Mischungsverhältnisse an der Messstelle beobachtet (10^2 - 10^4 pptv). Mischungsverhältnisse biogener flüchtige Kohlenwasserstoffverbindungen (BVOC, engl.: biogenic volatile organic compounds) aus dem umgebenden Wald (hauptsächlich Nadelwald) lagen in der Größenordnung 10^2 pptv vor. Die Charakteristiken des photostationären Gleichgewichtszustandes von NOx bei niedrigen NOx-Mischungsverhältnissen (10 - 10^3 pptv) wurde für eine weitere Messstelle in einem borealen Waldgebiet während der Messkampagne HUMPPA-COPEC 2010 untersucht. HUMPPA–COPEC–2010 wurde im Sommer 2010 in der SMEARII-Station in Hyytiälä, Süd-Finnland, durchgeführt. Die charakteristischen Eigenschaften des photostationären Gleichgewichtszustandes von NOx in den beiden Waldgebieten werden in dieser Arbeit verglichen. Des Weiteren ermöglicht der umfangreiche Datensatz - dieser beinhaltet Messungen von relevanten Spurengasen für die Radikalchemie (OH, HO2), sowie der totalen OH-Reaktivität – das aktuelle Verständnis bezüglich der NOx-Photochemie unter Verwendung von einem Boxmodell, in welches die gemessenen Daten als Randbedingungen eingehen, zu überprüfen und zu verbessern. Während NOx-Konzentrationen in HUMPPA-COPEC 2010 niedriger sind, im Vergleich zu PARADE 2011 und BVOC-Konzentrationen höher, sind die Zyklierungsprozesse von NO und NO2 in beiden Fällen grundlegend verstanden. Die Analyse des photostationären Gleichgewichtszustandes von NOx für die beiden stark unterschiedlichen Messstandorte zeigt auf, dass potenziell unbekannte Prozesse in keinem der beiden Fälle vorhanden sind. Die aktuelle Darstellung der NOx-Chemie wurde für HUMPPA-COPEC 2010 unter Verwendung des chemischen Mechanismus MIM3* simuliert. Die Ergebnisse der Simulation sind konsistent mit den Berechnungen basierend auf dem photostationären Gleichgewichtszustand von NOx.

CO Oxidation on Pt(100): New Insights based on Combined Voltammetric, Microscopic and Spectroscopic Experiments

We present an experimental study of the CO electro-oxidation on Pt(100)-(1 × 1) electrodes employing electrochemical methods in combination with in situ scanning tunneling microscopy (STM) and shell-isolated nanoparticle enhanced Raman spectroscopy (SHINERS). We discussed the nature and stability of the active sites in the preignition region in the presence of dissolved CO (COb) and monitored substrate structure changes during the COb electro-oxidation process. We corroborated that the electro-oxidation kinetics is determined decisively by the history of CO adlayer formation. A new mechanism was proposed for Pt(100) electrode deactivation in the preignition region after excursion of electrode potential to COb ignition region. We believe that this mechanism takes place on Pt surfaces independently on their crystallographic orientation.

Kinetics and Mechanism of Oxygen Delignification

Considerable research has been conducted into the kinetics and selectivity of the oxygen delignification process to overcome limitation in its use. However most studies were performed in a batch reactor whereby the hydroxide and dissolved oxygen concentrations are changing during the reaction time in an effort to simulate tower performance in pulp mills. This makes it difficult to determine the reaction order of the different reactants in the rate expressions. Also the lignin content and cellulose degradation of the pulp are only established at the end of the experiment when the sample is removed from the batch reactor. To overcome these deficiencies, we have adopted a differential reactor system used frequently for fluid-solid rate studies (so-called Berty reactor) for measurement of oxygen delignification kinetics. In this reactor, the dissolved oxygen concentration and the alkali concentration in the feed are kept constant, and the rate of lignin removal is determined from the dissolved lignin content in the outflow stream measured by UV absorption. The mass of lignin removed is verified by analyzing the pulp at several time intervals. Experiments were performed at different temperatures, oxygen pressures and caustic concentrations. The delignification rate was found to be first order in HexA-free residual lignin content. The delignification rate reaction order in caustic concentration and oxygen pressure were determined to be 0.42 and 0.44 respectively. The activation energy was found to be 53kJ/mol. The carbohydrate degradation during oxygen delignification can be described by two contributions: one due to radicals produced by phenolic delignification, and a much smaller contribution due to alkaline hydrolysis. From the first order of the reaction and the pKa of the active lignin site, a new oxygen delignification mechanism is proposed. The number 3 carbon atom in the aromatic ring with the attached methoxyl group forms the lignin active site for oxygen adsorption and subsequent electrophic reaction to form a hydroperoxide with a pKa value similar to that of the present delignification kinetics. The uniform presence of the aromatic methoxyl groups in residual lignin further support the first order in lignin kinetics.

The regulation of protein kinase C by thiol oxidation

The Ser/Thr protein kinase C (PKC) isozyme family plays an important role in cell growth and differentiation and also contributes to key events in the development and progression of cancer. PKC isozymes are activated by phospholipid-dependent mechanisms, and they are also subject to oxidative activation and inactivation. Oxidative regulatory mechanisms are important in the governance of PKC isozyme action. While oxidative PKC activation involves phospho-tyrosine (P-Y) stabilization, the molecular mechanism(s) for oxidative PKC inactivation have not been defined. We previously reported that Thr → Cys peptide-substrate analogs inactivate several PKC isozymes including PKC-α via S-thiolation, i.e., by forming disulfides with PKC thiols. This inactivation mechanism is chemically analogous to protein S-glutathiolation, a post-translational modification that has been shown to oxidatively regulate several enzymes. To determine if PKC-α could be inactivated by S-glutathiolation, we employed the thiol-specific oxidant diamide (0.01–10mM) and 100μM glutathione (GSH). Diamide alone (0.1–5.0 mM) weakly inactivated PKC-α (<20%), and GSH alone had no effect on the isozyme activity. Marked potentiation of diamide-induced PKC-α inactivation (>90%) was achieved by 100μM GSH, resulting in full inactivation of the isozyme. Inactivation was reversed by DTT, consistent with a mechanism involving PKC-α S-glutathiolation. S-glutathiolation was demonstrated as DTT-reversible incorporation of [35S] GSH into PKC-α isozyme structure. These results indicate that a mild oxidative stimulus can inactivate purified PKC-α via S-glutathiolation. In addition, diamide treatment of metabolically labeled NIH3T3 cells induced potent PKC-α inactivation via isozyme [35S] S-thiolation. These results indicate that cellular PKC-α can be regulated via S-glutathiolation. ^

Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H2O2

Amyotrophic lateral sclerosis (ALS) involves the progressive degeneration of motor neurons in the spinal cord and motor cortex. Mutations to Cu,Zn superoxide dismutase (SOD) linked with familial ALS are reported to increase hydroxyl radical adduct formation from hydrogen peroxide as measured by spin trapping with 5,5′-dimethyl-1-pyrrolline N-oxide (DMPO). In the present study, we have used oxygen-17-enriched water and H2O2 to reinvestigate the mechanism of DMPO/⋅OH formation from the SOD and SOD mutants. The relative ratios of DMPO/⋅17OH and DMPO/⋅16OH formed in the Fenton reaction were 90% and 10%, respectively, reflecting the ratios of H217O2 to H216O2. The reaction of the WT SOD with H217O2 in bicarbonate/CO2 buffer yielded 63% DMPO/⋅17OH and 37% DMPO/⋅16OH. Similar results were obtained from the reaction between familial ALS SOD mutants and H217O2: DMPO/⋅17OH (64%); DMPO/⋅16OH (36%) from A4V and DMPO/⋅17OH (62%); and DMPO/⋅16OH (38%) from G93A. These results were confirmed further by using 5-diethoxyphosphoryl-5-methyl-1-pyrroline N-oxide spin trap, a phosphorylated analog of DMPO. Contrary to earlier reports, the present results indicate that a significant fraction of DMPO/⋅OH formed during the reaction of SOD and familial ALS SOD mutants with H2O2 is derived from the incorporation of oxygen from water due to oxidation of DMPO to DMPO/⋅OH presumably via DMPO radical cation. No differences were detected between WT and mutant SODs, neither in the concentration of DMPO/⋅OH or DEPMPO/⋅OH formed nor in the relative incorporation of oxygen from H2O2 or water.

A mechanism of paraquat toxicity involving nitric oxide synthase

Paraquat (PQ) is a well described pneumotoxicant that produces toxicity by redox cycling with cellular diaphorases, thereby elevating intracellular levels of superoxide (O2⨪). NO synthase (NOS) has been shown to participate in PQ-induced lung injury. Current theory holds that NO reacts with O2⨪ generated by PQ to produce the toxin peroxynitrite. We asked whether NOS might alternatively function as a PQ diaphorase and reexamined the question of whether NO/O2⨪ reactions were toxic or protective. Here, we show that: (i) neuronal NOS has PQ diaphorase activity that inversely correlates with NO formation; (ii) PQ-induced endothelial cell toxicity is attenuated by inhibitors of NOS that prevent NADPH oxidation, but is not attenuated by those that do not; (iii) PQ inhibits endothelium-derived, but not NO-induced, relaxations of aortic rings; and (iv) PQ-induced cytotoxicity is potentiated in cytokine-activated macrophages in a manner that correlates with its ability to block NO formation. These data indicate that NOS is a PQ diaphorase and that toxicity of such redox-active compounds involves a loss of NO-related activity.

Modulation of potassium channel function by methionine oxidation and reduction

Oxidation of amino acid residues in proteins can be caused by a variety of oxidizing agents normally produced by cells. The oxidation of methionine in proteins to methionine sulfoxide is implicated in aging as well as in pathological conditions, and it is a reversible reaction mediated by a ubiquitous enzyme, peptide methionine sulfoxide reductase. The reversibility of methionine oxidation suggests that it could act as a cellular regulatory mechanism although no such in vivo activity has been demonstrated. We show here that oxidation of a methionine residue in a voltage-dependent potassium channel modulates its inactivation. When this methionine residue is oxidized to methionine sulfoxide, the inactivation is disrupted, and it is reversed by coexpression with peptide methionine sulfoxide reductase. The results suggest that oxidation and reduction of methionine could play a dynamic role in the cellular signal transduction process in a variety of systems.

Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase

The ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone (PQQ), semiquinone (PQQH), and dihydroquinone (PQQH2) have been determined and compared with ab initio structures of the (PQQ)Ca2+, (PQQH)Ca2+, and (PQQH2)Ca2+ complexes as well as the x-ray structure of (PQQ)Ca2+ bound at the active site of the methanol dehydrogenase (MDH) of methyltropic bacteria. Plausible mechanisms for the MDH oxidation of methanol involving the (PQQ)Ca2+ complex are explored via ab initio computations and discussed. Considering the reaction of methanol with PQQ in the absence of Ca2+, nucleophilic addition of methanol to the PQQ C-5 carbonyl followed by a retro-ene elimination is deemed unlikely due to large energy barrier. A much more favorable disposition of the methanol C-5 adduct to provide formaldehyde involves proton ionization of the intermediate followed by elimination of methoxide concerted with hydride transfer to the oxygen of the C-4 carbonyl. Much the same transition state is reached if one searches for the transition state beginning with Asp-303–CO2−general-base removal of the methanol proton of the (PQQ)Ca2+O(H)CH3 complex concerted with hydride transfer to the oxygen at C-4. For such a mechanism the role of the Ca2+ moiety would be to (i) contribute to the formation of the ES complex (ii) provide a modest decrease in the pKa of methanol substrate,; and (iii) polarize the oxygen at C-5.

Nitration of γ-tocopherol and oxidation of α-tocopherol by copper-zinc superoxide dismutase/H2O2/NO2−: Role of nitrogen dioxide free radical

Copper-zinc superoxide dismutase (Cu,ZnSOD) is the antioxidant enzyme that catalyzes the dismutation of superoxide (O2•−) to O2 and H2O2. In addition, Cu,ZnSOD also exhibits peroxidase activity in the presence of H2O2, leading to self-inactivation and formation of a potent enzyme-bound oxidant. We report in this study that lipid peroxidation of l-α-lecithin liposomes was enhanced greatly during the SOD/H2O2 reaction in the presence of nitrite anion (NO2−) with or without the metal ion chelator, diethylenetriaminepentacetic acid. The presence of NO2− also greatly enhanced α-tocopherol (α-TH) oxidation by SOD/H2O2 in saturated 1,2-dilauroyl-sn-glycero-3-phosphatidylcholine liposomes. The major product identified by HPLC and UV-studies was α-tocopheryl quinone. When 1,2-diauroyl-sn-glycero-3-phosphatidylcholine liposomes containing γ-tocopherol (γ-TH) were incubated with SOD/H2O2/NO2−, the major product identified was 5-NO2-γ-TH. Nitrone spin traps significantly inhibited the formation of α-tocopheryl quinone and 5-NO2-γ-TH. NO2− inhibited H2O2-dependent inactivation of SOD. A proposed mechanism of this protection involves the oxidation of NO2− by an SOD-bound oxidant to the nitrogen dioxide radical (•NO2). In this study, we have shown a new mechanism of nitration catalyzed by the peroxidase activity of SOD. We conclude that NO2− is a suitable probe for investigating the peroxidase activity of familial Amyotrophic Lateral Sclerosis-linked SOD mutants.

Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion

Mammalian xanthine oxidoreductases, which catalyze the last two steps in the formation of urate, are synthesized as the dehydrogenase form xanthine dehydrogenase (XDH) but can be readily converted to the oxidase form xanthine oxidase (XO) by oxidation of sulfhydryl residues or by proteolysis. Here, we present the crystal structure of the dimeric (Mr, 290,000) bovine milk XDH at 2.1-Å resolution and XO at 2.5-Å resolution and describe the major changes that occur on the proteolytic transformation of XDH to the XO form. Each molecule is composed of an N-terminal 20-kDa domain containing two iron sulfur centers, a central 40-kDa flavin adenine dinucleotide domain, and a C-terminal 85-kDa molybdopterin-binding domain with the four redox centers aligned in an almost linear fashion. Cleavage of surface-exposed loops of XDH causes major structural rearrangement of another loop close to the flavin ring (Gln 423—Lys 433). This movement partially blocks access of the NAD substrate to the flavin adenine dinucleotide cofactor and changes the electrostatic environment of the active site, reflecting the switch of substrate specificity observed for the two forms of this enzyme.

Bromination of deoxycytidine by eosinophil peroxidase: A mechanism for mutagenesis by oxidative damage of nucleotide precursors

Oxidants generated by eosinophils during chronic inflammation may lead to mutagenesis in adjacent epithelial cells. Eosinophil peroxidase, a heme enzyme released by eosinophils, generates hypobromous acid that damages tissue in inflammatory conditions. We show that human eosinophils use eosinophil peroxidase to produce 5-bromodeoxycytidine. Flow cytometric, immunohistochemical, and mass spectrometric analyses all demonstrated that 5-bromodeoxycytidine generated by eosinophil peroxidase was taken up by cultured cells and incorporated into genomic DNA as 5-bromodeoxyuridine. Although previous studies have focused on oxidation of chromosomal DNA, our observations suggest another mechanism for oxidative damage of DNA. In this scenario, peroxidase-catalyzed halogenation of nucleotide precursors yields products that subsequently can be incorporated into DNA. Because the thymine analog 5-BrUra mispairs with guanine in DNA, generation of brominated pyrimidines by eosinophils might constitute a mechanism for cytotoxicity and mutagenesis at sites of inflammation.

Identification of a Saccharomyces cerevisiae Gene that Is Required for G1 Arrest in Response to the Lipid Oxidation Product Linoleic Acid Hydroperoxide*

Reactive oxygen species cause damage to all of the major cellular constituents, including peroxidation of lipids. Previous studies have revealed that oxidative stress, including exposure to oxidation products, affects the progression of cells through the cell division cycle. This study examined the effect of linoleic acid hydroperoxide, a lipid peroxidation product, on the yeast cell cycle. Treatment with this peroxide led to accumulation of unbudded cells in asynchronous populations, together with a budding and replication delay in synchronous ones. This observed modulation of G1 progression could be distinguished from the lethal effects of the treatment and may have been due to a checkpoint mechanism, analogous to that known to be involved in effecting cell cycle arrest in response to DNA damage. By examining several mutants sensitive to linoleic acid hydroperoxide, the YNL099c open reading frame was found to be required for the arrest. This gene (designated OCA1) encodes a putative protein tyrosine phosphatase of previously unknown function. Cells lacking OCA1 did not accumulate in G1 on treatment with linoleic acid hydroperoxide, nor did they show a budding, replication, or Start delay in synchronous cultures. Although not essential for adaptation or immediate cellular survival, OCA1 was required for growth in the presence of linoleic acid hydroperoxide, thus indicating that it may function in linking growth, stress responses, and the cell cycle. Identification of OCA1 establishes cell cycle arrest as an actively regulated response to oxidative stress and will enable further elucidation of oxidative stress-responsive signaling pathways in yeast.

Evidence of Local pH Changes during Ethanol Oxidation at Pt Electrodes in Alkaline Media

Local changes of the interfacial pH can significantly affect the rate and mechanism during the course of an electrodic reaction. For instance, different pH values will have a significant effect on the equilibrium properties of both solution and surface species, altering the reactions kinetics. Ethanol oxidation at platinum electrodes in alkaline media involves the fast consumption of OH− species that will change the local pH at the electrode surface, decreasing the reaction rate. In this study, the local pH change during ethanol oxidation in alkaline media is accomplished by using rotating ring-disc electrode (RRDE) experiments. The current at the ring when polarized at the onset of hydrogen evolution serves as a measure of the local pH in the vicinity of the electrode. The results show that the current at the ring at 0.1 V (vs. RHE) becomes more negative during ethanol oxidation, owing to a change in the equilibrium potential of the hydrogen evolution reaction caused by a change in the local pH.