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An organophosphorus ‐catalyzed method for the direct electrophilic cyanation of C(sp2)−H nucleophiles with sodium cyanate (NaOCN) is reported. The catalytic deoxyfunctionalization of the OCN− anion is enabled by the use of a small‐ring phosphacyclic (phosphetane) catalyst in combination with a terminal hydrosilane O‐atom acceptor and a malonate‐derived bromenium donor. In situ spectroscopy under single‐turnover conditions demonstrate that insoluble inorganic cyanate anion is activated by bromide displacement on a bromophosphonium catalytic intermediate to give a reactive N‐bound isocyanatophosphonium ion, which delivers electrophilic "CN+" equivalents to nucleophilic (hetero)arenes and alkenes with loss of a phosphine oxide. These results demonstrate the feasibility of deoxyfunctionalization of insoluble inorganic salts by PIII/PV=O catalyzed phase transfer activation. [ABSTRACT FROM AUTHOR]

Cyanate, a toxic product from the chemical oxidation treatment of highly toxic cyanide, can be converted to harmless ammonia and carbon dioxide by cyanase (EC 4.2.1.104). Cyanase from Thermomyces lanuginosus was entrapped in biomimetic silica to improve stability and reusability. After entrapment, the enzyme's activity increased by two-fold, and the residual activity after 30-min of incubation at 60 °C also increased by two-fold, compared to the free enzyme. After being stored at room temperature for 28 days, the entrapped cyanase retained 79% of the initial activity, while the free form retained 61%. The immobilized cyanase was successfully applied to cyanate detoxification; the co-entrapment of carbonic anhydrase from Sulfurihydrogenibium azorense decreased the amount of bicarbonate necessary for cyanate detoxification by 50%. The cyanate degradation retained 53% of the initial value after the co-entrapped cyanate and carbonic anhydrase were reused five times. [ABSTRACT FROM AUTHOR]

Introduction: Assimilation of reduced nitrogen is less energetically costly than assimilation of oxidized forms. In the open ocean, ammonium is generally absent from the water column, including in oxygen-deficient zones (ODZs). Some microorganisms can use alternative organic reduced nitrogen forms like urea and cyanate, as indicated by the presence of cyanase (cynS) and urease (ureC) genes. Methods: Here we examine the Hawaii Ocean Time series, two stations in the Eastern Tropical South Pacific ODZ and one in the Eastern Tropical North Pacific ODZ, using phylogenetic read placement of metagenomic reads to define the proportion of each taxon capable of using cyanate and/or urea in oxic and anoxic environments. Results: An improved phylogenetic tree found that Thioglobaceae and Verrucomicrobia had the capability to use urea. Our detailed examination of all the microbial groups able to use cyanate and urea illuminated that niche differentiation, an adaptation to minimize competition, determines chosen nitrogen sources, partitioning by depth and oxygen. Urease genes were found in Picocyanobacteria and SAR11 in surface waters, Thaumarchaeota and Nitrospina in deep waters, Thioglobaceae and Cand. Scalindua in ODZs, and Verrucomicrobia in the deep oxycline. In the ODZs, the percentage of Anammox bacteria that contained cynS was double that of those containing ureC, and their cynS transcripts were abundant, indicating a preference for cyanate over urea. Discussion: While Prochlorococcus could utilize cyanate in the deep chlorophyll maximum, in the ODZs, Prochlorococcus uses nitrite rather than compete with Cand. Scalindua for cyanate, even though cyanate is present. SAR11 and Prochlorococcus may compete for urea in surface waters, but for SAR11, the presence of ureC was negatively correlated with nitrate concentration (p = 10-17), with ~ 40% of SAR11 genomes containing the ureC gene in oxic surface waters but none at depth, indicating that SAR11 bacteria switched to using nitrate when available. In the oxycline above the ODZ, where Thaumarchaeota and Nitrospina both could use urea, 50% of Nitrospina were also able to use cyanate, and their cyanase transcripts were present. This use of dissolved organic N should allow a higher biomass of N-cycling microbes and higher N-transformation rates than in a system competing for ammonia only. [ABSTRACT FROM AUTHOR]

Understanding nitrogen (N) uptake rates respect to nutrient availability and the biogeography of phytoplankton communities is crucial for untangling the complexities of marine ecosystems and the physical, biological, and chemical forces shaping them. In the summer of 2016, we conducted measurements of bulk microbial uptake rates for six 15N-labeled substrates: nitrate, nitrite, ammonium, urea, cyanate, and dissolve free amino acids across distinct marine provinces, including the continental shelf of the Mid-and South Atlantic Bights (MAB and SAB), the Slope Sea, and the Gulf Stream, marking the first instance of simultaneously measuring six different N uptake rates in this dynamic region. Total measured N uptake rates were lowest in the Gulf Stream followed by the SAB. Notably, the MAB exhibited significantly higher N uptake rates compared to the SAB, likely due to the excess levels of pre-existing phosphorus present in the MAB. Together, urea and nitrate uptake contributed approximately 50% of the total N uptake across the study region. Although cyanate uptake rates were consistently low, they accounted for up to 11% of the total measured N uptake at some Gulf Stream stations. Phytoplankton groups were identified based on specific pigment markers, revealing a dominance of diatoms in the shelf community, while Synechococcus, Prochlorococcus, and pico-eukaryotes dominated in oligotrophic Gulf Stream waters. The reported uptake rates in this study were mostly in agreement with previous studies conducted in coastal waters of the North Atlantic Ocean. This study suggests there are distinct regional patterns of N uptake in this physically dynamic region, correlating with nutrient availability and phytoplankton community composition. These findings contribute valuable insights into the intricate interplay of biological and chemical factors shaping N dynamics in disparate marine ecosystems. [ABSTRACT FROM AUTHOR]

IntroductionAssimilation of reduced nitrogen is less energetically costly than assimilation of oxidized forms. In the open ocean, ammonium is generally absent from the water column, including in oxygen-deficient zones (ODZs). Some microorganisms can use alternative organic reduced nitrogen forms like urea and cyanate, as indicated by the presence of cyanase (cynS) and urease (ureC) genes.MethodsHere we examine the Hawaii Ocean Time series, two stations in the Eastern Tropical South Pacific ODZ and one in the Eastern Tropical North Pacific ODZ, using phylogenetic read placement of metagenomic reads to define the proportion of each taxon capable of using cyanate and/or urea in oxic and anoxic environments.ResultsAn improved phylogenetic tree found that Thioglobaceae and Verrucomicrobia had the capability to use urea. Our detailed examination of all the microbial groups able to use cyanate and urea illuminated that niche differentiation, an adaptation to minimize competition, determines chosen nitrogen sources, partitioning by depth and oxygen. Urease genes were found in Picocyanobacteria and SAR11 in surface waters, Thaumarchaeota and Nitrospina in deep waters, Thioglobaceae and Cand. Scalindua in ODZs, and Verrucomicrobia in the deep oxycline. In the ODZs, the percentage of Anammox bacteria that contained cynS was double that of those containing ureC, and their cynS transcripts were abundant, indicating a preference for cyanate over urea.DiscussionWhile Prochlorococcus could utilize cyanate in the deep chlorophyll maximum, in the ODZs, Prochlorococcus uses nitrite rather than compete with Cand. Scalindua for cyanate, even though cyanate is present. SAR11 and Prochlorococcus may compete for urea in surface waters, but for SAR11, the presence of ureC was negatively correlated with nitrate concentration (p = 10−17), with ~ 40% of SAR11 genomes containing the ureC gene in oxic surface waters but none at depth, indicating that SAR11 bacteria switched to using nitrate when available. In the oxycline above the ODZ, where Thaumarchaeota and Nitrospina both could use urea, 50% of Nitrospina were also able to use cyanate, and their cyanase transcripts were present. This use of dissolved organic N should allow a higher biomass of N-cycling microbes and higher N-transformation rates than in a system competing for ammonia only.

Cyanate is a nitrogen and energy source for diverse marine microorganisms, playing important roles in the nitrogen cycle. Despite the extensive research on cyanate utilization, the sources of this nitrogen compound remain largely enigmatic. To unravel the sources of cyanate, distributions and production of cyanate during photochemical degradation of natural dissolved organic matter (DOM) were investigated across various environments, including freshwater, estuarine, coastal areas in Florida, and the continental and slope regions of the North American mid-Atlantic Ocean (NATL). Cyanate production was also examined during the photochemical degradation of exudates from a typical strain of Synechococcus, an important phytoplankton component. To deepen our understanding of the sources and production mechanisms of cyanate, its production was assessed during the photochemical degradation of a natural seawater DOM supplemented with five nitrogen-containing compounds with distinguishing structures and functional groups. Generally, cyanate exhibited higher concentrations in the Florida coastal, estuarine, and freshwater environments than the NATL. However, cyanate distribution did not consistently align with its production rates. Despite significantly low concentrations in the NATL, DOM from this region exhibited cyanate production rates comparable to estuarine and Florida coastal environments. Although relatively high cyanate concentrations were observed in the freshwaters, DOM in this environment exhibited very low cyanate production rates. A highly significant correlation was observed between cyanate and chlorophyll a (Chl a) concentrations in these areas. Moreover, in most estuarine and NATL stations, cyanate concentration and production rate in the Chl a maximum layer were significantly higher than in other layers. Cyanate was produced during the photochemical degradation of the Synechococcus exudates. The cyanate production was significantly enhanced when the natural seawater DOM was supplemented with GlycylGlycine, 4-(methylamino) benzoic acid, 4-[ethyl(methyl)amino] benzaldehyde or methyl 2-aminobenzoate. Our study implies that photochemical degradation of marine DOM, especially phytoplankton-derived DOM, is a substantial source of cyanate in the ocean. Additionally, cyanate may form during the degradation of peptides and small aromatic compounds in DOM, providing novel insights into the nitrogen cycle. [ABSTRACT FROM AUTHOR]

Ammonia-oxidizing archaea (AOA) and bacteria (AOB), nitrite-oxidizing bacteria (NOB), and complete ammonia oxidizers (comammox) are responsible for nitrification in nature; however, some groups have been reported to utilize labile-dissolved organic nitrogen (LDON) for satisfying nitrogen demands. To understand the universality of their capacity of LDON metabolism, we collected 70 complete genomes of AOA, AOB, NOB, and comammox from typical environments for exploring their potentials in the metabolism of representative LDON (urea, polyamines, cyanate, taurine, glycine betaine, and methylamine). Genomic analyses showed that urea was the most popular LDON used by nitrifiers. Each group harbored unique urea transporter genes (AOA: dur3 and utp, AOB: utp, and NOB and comammox: urtABCDE and utp) accompanied by urease genes ureABC. The differentiation in the substrate affinity of these transporters implied the divergence of urea utilization efficiency in nitrifiers, potentially driving them into different niches. The cyanate transporter (cynABD and focA/nirC) and degradation (cynS) genes were detected mostly in NOB, indicating their preference for a wide range of nitrogen substrates to satisfy high nitrogen demands. The lack of genes involved in the metabolism of polyamines, taurine, glycine betaine, and methylamines in most of nitrifiers suggested that they were not able to serve as a source of ammonium, only if they were degraded or oxidized extracellularly as previously reported. The phylogenetic analyses assisted with comparisons of GC% and the Codon Adaptation Index between target genes and whole genomes of nitrifiers implied that urea metabolic genes dur3 and ureC in AOA evolved independently from bacteria during the transition from Thaumarchaeota to AOA, while utp in terrestrial AOA was acquired from bacteria via lateral gene transfer (LGT). Cyanate transporter genes cynS and focA/nirC detected only in a terrestrial AOA Candidadus Nitrsosphaera gargensis Ga9.2 could be gained synchronously with Nitrospira of NOB by an ancient LGT. Our results indicated that LDON utilization was a common feature in nitrifiers, but metabolic potentials were different among nitrifiers, possibly being intensely interacted with their niches, survival strategies, and evolutions. [ABSTRACT FROM AUTHOR]

The reaction condition for purifying carbonic anhydrase from Sulfurihydrogenibium yellowstonense (SspCA) by direct heating without prior cell lysis was optimized; heating at 70 °C for 5 min resulted in the highest total activity of 23,460 WAU (Wilbur–Anderson unit) from a 50 mL culture. Heat-purified SspCA was examined for its capability to increase the rate of the mineralization of CO2; compared with an uncatalyzed control, the onset time of CaCO3 formation was shortened by up to 71%. Cyanase can be used to degrade toxic cyanate; however, one of the limitations of this biomimetic process is that the reaction needs HCO3− as a substrate. Heat-purified SspCA was combined with heat-purified cyanase from Thermomyces lanuginosus to alleviate the HCO3− dependence; in industrial wastewater, the HCO3− required was reduced by 50% when 0.75 WAU of SspCA was added. Heat-purified SspCA is stable at 4 °C; 88% of the initial activity was retained for up to five weeks. Partially purified SspCA can be obtained with ease and applied to a variety of applications. [ABSTRACT FROM AUTHOR]

Cyanate is a simple nitrogen-containing organic compound that occurs in surface water at subnanomolar to nanomolar concentrations. To examine the possibility of cyanate as a source of nitrogen for phytoplankton populations in the nitrogen-limiting surface waters of the North Pacific Subtropical Gyre, we conducted enrichment experiments at three stations along the longitudinal transect at 23° N. All three phytoplankton populations, Prochlorococcus, Synechococcus, and eukaryotic phytoplankton, were stressed by nitrogen deficiency throughout the transect, and their responses to cyanate enrichment varied with phytoplankton populations and stations. Although Prochlorococcus responded positively to cyanate enrichment, the increases in its cellular chlorophyll fluorescence and cell concentration were significantly smaller than those under ammonium-enriched conditions (p < 0.05), suggesting its considerable but limited accessibility to cyanate. In contrast, Synechococcus showed a distinct response to cyanate enrichment in the central Pacific, which was indistinguishable from that observed under ammonium-enriched conditions, suggesting its high capability to utilize cyanate as an alternative nitrogen source. Contrary to these two pico-cyanobacterial populations, eukaryotic pico- and nanophytoplankton showed almost no significant response to cyanate addition. The present study results demonstrate that cyanate can be an alternative nitrogen source for pico-sized cyanobacteria in the subtropical North Pacific, particularly in the central North Pacific, where nitrogen is the single limiting factor for growth. [ABSTRACT FROM AUTHOR]

A green and low-cost removal method for cyanate, a toxic byproduct from the treatment of cyanide, is still needed. Cyanase converts cyanate to CO2 and NH3, but its industrial practicality is limited because the reaction requires HCO3− as a substrate. In this study, we used carbonic anhydrase from Sulfurihydrogenibium azorense (SazCA) to provide HCO3− for cyanase from Thermomyces lanuginosus (TlCyn); both TlCyn and SazCA were purified by one-step heating without prior cell lysis. The heat treatment resulted in higher activities of both enzymes than the conventional two-step process. From a 50 mL-culture, the highest total activity of 147 U and 47,174 WAU was obtained from 5 min of heating at 60 and 80 °C for TlCyn and SazCA, respectively. The coupled enzymatic system was used to degrade cyanate in three different matrices: 50 mM Tris-HCl (pH 8), industrial wastewater, and artificial wastewater. In the industrial wastewater, with the addition of 0.75 WAU (Wilbur-Anderson unit) of SazCA, cyanate degradation using 0.5 mM NaHCO3 was similar to that using 3 mM NaHCO3, indicating an 83% reduction in NaHCO3. We have demonstrated that the dependence on HCO3− of cyanate degradation can be effectively alleviated by using low-cost heat-purified TlCyn and SazCA; the industrial practicality of the coupled enzymatic system is therefore improved. [ABSTRACT FROM AUTHOR]

Introduction: Chronic cassava-derived cyanide poisoning is associated with the appearance of konzo, a tropical spastic paraparesis due to selective upper motor neuron damage. Whether the disease is caused by a direct action of cyanide or its metabolites is still an open question. This preliminary study assessed the neurotoxic effects of thiocyanate (SCN) and cyanate (OCN), two cyanide metabolites hypothesized to be plausible toxic agents in konzo., Methods: Cultured mouse neuroblastoma (Neuro-2A) and human neuroblastoma (SH-SY5Y) cell lines were incubated (24, 48, and 72 hours) in sodium OCN or sodium SCN in a disease-relevant concentration range. Cell viability, caspase (3, 8, and 9) activities, and reactive oxygen species (ROS) generation were evaluated using appropriate assay kits. Additionally, electrophysiological responses induced by OCN and SCN in primary spinal cord neurons (from Sprague Dawley rats) were assessed by whole-cell patch-clamp techniques., Results: Both OCN and SCN were toxic in a dose-dependent way, even if SCN toxicity appeared at very high concentrations (30 mM, corresponding to more than 100-fold higher than normal plasmatic levels), contrary to OCN (0.3-3 mM). OCN was markedly more toxic in a poor culture medium (MEM; IC50 = 3.2 mM) compared to a glucose- and amino acid-rich medium (DMEM; IC50=7.6 mM). OCN treatment increased the ROS generation by 8.9 folds, as well as the Caspase-3, Caspase-8, and Caspase-9 activities by 3.2, 2.5, and 2.6 folds, respectively. Finally, OCN (and SCN to a lesser extent) induced depolarizing currents in primary spinal cord neurons, through an activation of ionotropic glutamate receptors., Conclusion: Our results suggest OCN as the most plausible neurotoxic agent involved in konzo, while SCN toxicity could be questioned at such high concentrations. Also, they support apoptosis, oxidative stress, and excitotoxicity as probable mechanisms of OCN neurotoxicity., Competing Interests: Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Marius Baguma reports financial support was provided by VLIR-UOS Team Project 2017 (Ref. No. CD2017TEA439A104), by The Board of Directors of UHasselt (Special Research Fund, BOF 2017 - Bilateral Scientific Cooperation. Ref. BOF17BL19), and by by The Doctoral Schools of UHasselt (Doctoral Schools Mobility grant - call 1 2020). The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript; or in the decision to publish the results. The other authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The reaction condition for purifying carbonic anhydrase from Sulfurihydrogenibium yellowstonense (SspCA) by direct heating without prior cell lysis was optimized; heating at 70 °C for 5 min resulted in the highest total activity of 23,460 WAU (Wilbur–Anderson unit) from a 50 mL culture. Heat-purified SspCA was examined for its capability to increase the rate of the mineralization of CO2; compared with an uncatalyzed control, the onset time of CaCO3 formation was shortened by up to 71%. Cyanase can be used to degrade toxic cyanate; however, one of the limitations of this biomimetic process is that the reaction needs HCO3− as a substrate. Heat-purified SspCA was combined with heat-purified cyanase from Thermomyces lanuginosus to alleviate the HCO3− dependence; in industrial wastewater, the HCO3− required was reduced by 50% when 0.75 WAU of SspCA was added. Heat-purified SspCA is stable at 4 °C; 88% of the initial activity was retained for up to five weeks. Partially purified SspCA can be obtained with ease and applied to a variety of applications.

Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing (pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized (pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation reactions with cell and tissue constituents. The present article reviews basic biochemical and redox mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases. Thyroid peroxidase and peroxidasin are key enzymes for thyroid hormone synthesis and the formation of functional cross-links in collagen IV during basement membrane formation. Special attention is directed to the properties, enzymatic mechanisms, and resulting (pseudo)halogenated products of the immunologically relevant proteins such as myeloperoxidase, eosinophil peroxidase, and lactoperoxidase. The potential role of the (pseudo)halogenated products (hypochlorous acid, hypobromous acid, hypothiocyanite, and cyanate) of these three heme peroxidases is further discussed. [ABSTRACT FROM AUTHOR]

Inorganic anions inhibit the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) generally by coordinating to the active site metal ion. Cyanate was reported as a non-coordinating CA inhibitor but those erroneous results were subsequently corrected by another group. We review the anion CA inhibitors (CAIs) in the more general context of drug design studies and the discovery of a large number of inhibitor classes and inhibition mechanisms, including zinc binders (sulphonamides and isosteres, dithiocabamates and isosteres, thiols, selenols, benzoxaboroles, ninhydrins, etc.); inhibitors anchoring to the zinc-coordinated water molecule (phenols, polyamines, sulfocoumarins, thioxocoumarins, catechols); CAIs occluding the entrance to the active site (coumarins and derivatives, lacosamide), as well as compounds that bind outside the active site. All these new chemotypes integrated with a general procedure for obtaining isoform-selective compounds (the tail approach) has resulted, through the guidance of rigorous X-ray crystallography experiments, in the development of highly selective CAIs for all human CA isoforms with many pharmacological applications.

An organophosphorus -catalyzed method for the direct electrophilic cyanation of C(sp 2 )-H nucleophiles with sodium cyanate (NaOCN) is reported. The catalytic deoxyfunctionalization of the OCN - anion is enabled by the use of a small-ring phosphacyclic (phosphetane) catalyst in combination with a terminal hydrosilane O-atom acceptor and a malonate-derived bromenium donor. In situ spectroscopy under single-turnover conditions demonstrate that insoluble inorganic cyanate anion is activated by bromide displacement on a bromophosphonium catalytic intermediate to give a reactive N-bound isocyanatophosphonium ion, which delivers electrophilic "CN + " equivalents to nucleophilic (hetero)arenes and alkenes with loss of a phosphine oxide. These results demonstrate the feasibility of deoxyfunctionalization of insoluble inorganic salts by P III /P V =O catalyzed phase transfer activation., (© 2024 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.)

Inorganic anions inhibit the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) generally by coordinating to the active site metal ion. Cyanate was reported as a non-coordinating CA inhibitor but those erroneous results were subsequently corrected by another group. We review the anion CA inhibitors (CAIs) in the more general context of drug design studies and the discovery of a large number of inhibitor classes and inhibition mechanisms, including zinc binders (sulphonamides and isosteres, dithiocabamates and isosteres, thiols, selenols, benzoxaboroles, ninhydrins, etc.); inhibitors anchoring to the zinc-coordinated water molecule (phenols, polyamines, sulfocoumarins, thioxocoumarins, catechols); CAIs occluding the entrance to the active site (coumarins and derivatives, lacosamide), as well as compounds that bind outside the active site. All these new chemotypes integrated with a general procedure for obtaining isoform-selective compounds (the tail approach) has resulted, through the guidance of rigorous X-ray crystallography experiments, in the development of highly selective CAIs for all human CA isoforms with many pharmacological applications. [ABSTRACT FROM AUTHOR]

From an engineering practical perspective, modification, thermal analysis for curing properties of cyanate ester resin, as well as development of adhesives and composites based on cyanate ester resin are reviewed. Modification of cyanate involves toughening by rubbers or thermoplastics, synergistic modification with epoxy and bismaleimide, and so on. The adhesive development examination results show that the satisfied lap shear strength and peel strength are gained by using hydroxyl-terminated poly (ether sulfone) (PES-OH), and moreover, relative lower dielectric constant and lower loss tangent are maintained. Although the strength can be improved by adding epoxy, such kind adhesive composition still has relative poor electrical properties. The developed cyanate adhesive SY-CN has higher lap shear strengths up to 30 MPa at temperatures below 175 ℃, lower dielectric loss of 0.0065, unchanged strength level after 200 hours of hot-aging at 200 ℃, and satisfied anti-peel performance, e.g. sandwich honeycomb climbing drum peel strength is up to 83.2 N?mm/mm. More and more studies on cure kinetic thermal analysis have indicated that the increase or decrease in curing activation energy data of modified cyanate ester resin versus unmodified cyanate ester resin can be synchronized with up or down of maximum cure peak temperature from the differential scanning calorimetry (DSC) curves, and also can be changed oppositely. Cyanate ester resin modified with hydroxyl-terminated poly (ether sulfone) (PES-OH) has lower maximum cure peak temperature of about 20 ℃ reduction versus unmodified cyanate, but the curing activation energy increase which can be due to change of reaction mechanism and steric hindrance effect. Based on change of maximum cure peak temperatures (Tp) with different heating rate data (?) from DSC curves, a linear equation of Tp = T1 + ΔT ln ? has been established, then, the curing temperature parameter can be more reasonably determined.

Method of determination of potassium cyanate in carbamylated darbepoietin alpha drug substance was developed. The method is based on derivatization of cyanate by methyl ester of anthranilic acid followed by formation bicyclic derivative (1-H,3-H-quinazolinedione), which is able to fluorescence. Application of this method to determine potassium cyanate in protein drugs was investigated. Interference of excipients on this method was evaluated. The validation was performed: specificity, linearity, accuracy, precision, limit of quantitication.

Electrochemical alternating current synthesis starting from an ethanol solution of CuSO4 · 5H2O and allylamine in the presence of solid sodium azide results in formation of Cu[C3H5NH2]N3. The trigonal-pyramidal coordination environment of both crystallographically independent copper ions consists of the C = C-bond of one allylamine molecule, the NH2-group of another ligand moiety and two N-atoms of the two azide-anions. One N3− exhibits a terminal coordination mode and the other is a μ3-1,1,3-bridge. The bridging function of both allylamine and azide leads to formation of a complicated 3-D network. An elongation of coordinated C = C-bond and a strong shift of the νs mode in the Raman spectrum confirm effective Cu–(C = C) bonding. A similar synthetic route starting from a methanol solution of Cu(BF4)2 · 6H2O in the presence of solid potassium cyanate results in formation of Cu[C3H5NH2]NCO. The cyanate-anion is bound to copper through nitrogen. The nitrogen from the allylamine molecule and the C = C-bond from another ligand complete the trigonal-planar environment of copper. The elongation of the coordinated C = C-bond and the shift of νs (C = C) mode in the Raman spectrum are similar to those in the azide derivative. [ABSTRACT FROM AUTHOR]

Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing (pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized (pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation reactions with cell and tissue constituents. The present article reviews basic biochemical and redox mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases. Thyroid peroxidase and peroxidasin are key enzymes for thyroid hormone synthesis and the formation of functional cross-links in collagen IV during basement membrane formation. Special attention is directed to the properties, enzymatic mechanisms, and resulting (pseudo)halogenated products of the immunologically relevant proteins such as myeloperoxidase, eosinophil peroxidase, and lactoperoxidase. The potential role of the (pseudo)halogenated products (hypochlorous acid, hypobromous acid, hypothiocyanite, and cyanate) of these three heme peroxidases is further discussed.

Understanding nitrogen (N) uptake rates respect to nutrient availability and the biogeography of phytoplankton communities is crucial for untangling the complexities of marine ecosystems and the physical, biological, and chemical forces shaping them. In the summer of 2016, we conducted measurements of bulk microbial uptake rates for six 15 N-labeled substrates: nitrate, nitrite, ammonium, urea, cyanate, and dissolve free amino acids across distinct marine provinces, including the continental shelf of the Mid-and South Atlantic Bights (MAB and SAB), the Slope Sea, and the Gulf Stream, marking the first instance of simultaneously measuring six different N uptake rates in this dynamic region. Total measured N uptake rates were lowest in the Gulf Stream followed by the SAB. Notably, the MAB exhibited significantly higher N uptake rates compared to the SAB, likely due to the excess levels of pre-existing phosphorus present in the MAB. Together, urea and nitrate uptake contributed approximately 50% of the total N uptake across the study region. Although cyanate uptake rates were consistently low, they accounted for up to 11% of the total measured N uptake at some Gulf Stream stations. Phytoplankton groups were identified based on specific pigment markers, revealing a dominance of diatoms in the shelf community, while Synechococcus , Prochlorococcus , and pico-eukaryotes dominated in oligotrophic Gulf Stream waters. The reported uptake rates in this study were mostly in agreement with previous studies conducted in coastal waters of the North Atlantic Ocean. This study suggests there are distinct regional patterns of N uptake in this physically dynamic region, correlating with nutrient availability and phytoplankton community composition. These findings contribute valuable insights into the intricate interplay of biological and chemical factors shaping N dynamics in disparate marine ecosystems., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The author(s) declared that they were an editorial board member of Frontiers, at the time of submission. This had no impact on the peer review process and the final decision., (Copyright © 2024 Zhu, Mulholland, Bernhardt, Neeley, Widner, Tapia and Echevarria.)

Organic compounds are employed as additives to increase the dissolution speed of gold, in concentrations around 1 g/L when using cyanidation, thereby forming a residual aqueous effluent with high amounts of free cyanides and organic compounds, which generate metallic complexes difficult to degrade. To increase the photodegradation efficiency, promising niobium and titanium porous materials are proposed as photocatalysts, due to their role in simultaneous oxidation and reduction reactions. In the process of cyanide oxidation, NbO5 0.3H2O was doped with titanium oxalate (IV) of 0.5, 1, and 1.5%; and HTiNbO5 were synthesized, from the mixture of NbO5 with TiO2 Degussa-P25, by coprecipitation, impregnation, and solid state. The determination of its elemental composition, morphological and textural properties were carried out by using various XRD techniques, Raman spectroscopy, SEM/EDS and acidity by pyridine. The experiments of photocatalytic oxidation of cyanide used one semibatch reactor with ultraviolet irradiation 125 W in a pH range of 9.5–12. The catalyst with the highest percentage of degradation was HTiNbO5 93.7%, which is attributed to the microstructure of the double layer and Lewis acidity sites, followed by NbTi-1% 92.9% and the Nb2O5.3H2O 82.4%, being the majority product cyanate, proposing its mechanism of reaction. Characterization experiments indicated Nb-O-Ti bridges that have been associated with the control of redox properties of the niobium species and Ti-O-Nb = O, which could be generating a greater number of e–H +pairs, increasing the photocatalytic activity. It is considered that the method of synthesis has a strong influence in changing the morphology of the particles such as porosity, specific surface and factors such as the acidity of niobium–based catalysts, which are important to achieving efficiency in degradation. Niobium-Titanium photocatalysts proved to be an excellent new breakthrough in Advanced Oxidation Technologies (AOT), to eliminate cyanide in wastewater from mining activities.

In order to enhance the moisture resistance of cyanate ester resins, modifiers containing silicon or fluorine moieties were introduced. The curing behaviors of the obtained resins, as well as thermal, water absorption, and dielectric properties of all cured polymers, were investigated in detail. Results show that properties of fillers in polymer have great influence on the thermal property and of polymer. In all cases, modifier exhibited percolation threshold at 5 wt%. Compared with pristine cyanate ester resins (CE), when the methyl phenyl silicone resin B filler was added, the cured polymer exhibited water absorption as low as 0.39% and excellent thermal oxygen stability at 300°C. The introduction of silicon H improved thermal oxidative stability at 400°C without significant compromise in processability or mechanical properties. [ABSTRACT FROM AUTHOR]

An efficient biocatalytic approach for enantio‐ and regioselective ring‐opening of styrene oxides with cyanate was developed by using the halohydrin dehalogenase HheC from Agrobacterium radiobacter AD1, generating the corresponding chiral 5‐aryl‐2‐oxazolidinones in up to 47% yield and 90% ee. Additionally, the origin of enantioselectivity and regioselectivity of the HheC‐catalyzed cyanate‐mediated ring‐opening process was uncovered by single enantiomer bioconversions and molecular docking study. [ABSTRACT FROM AUTHOR]

The compound Cs[OCN] has been synthesized and its crystal structure and Raman spectrum were determined on selected single crystals. As postulated in earlier work, the title compound crystallizes isopointal to KN3 exhibiting the space group I4/mcm (no. 140, Z = 4) with the lattice parameters a = 653.79(2) and c = 799.42(5) pm. The Raman spectrum verified the nature of the triatomic moiety and shows the frequencies typical for an [OCN]− anion with Fermi resonance between the 2δ and the νsym vibrations. The undisturbed frequencies and the resulting force constants have been calculated and compared to those of other alkali metal compounds containing comparable linear triatomic anions. [ABSTRACT FROM AUTHOR]

The genomes of Thiohalobacter thiocyanaticus and Guyparkeria (formerly known as Halothiobacillus) sp. SCN-R1, two gammaproteobacterial halophilic sulfur-oxidizing bacteria (SOB) capable of thiocyanate oxidation via the “cyanate pathway”, have been analyzed with a particular focus on their thiocyanate-oxidizing potential and sulfur oxidation pathways. Both genomes encode homologs of the enzyme thiocyanate dehydrogenase (TcDH) that oxidizes thiocyanate via the “cyanate pathway” in members of the haloalkaliphilic SOB of the genus Thioalkalivibrio. However, despite the presence of conservative motives indicative of TcDH, the putative TcDH of the halophilic SOB have a low overall amino acid similarity to the Thioalkalivibrio enzyme, and also the surrounding genes in the TcDH locus were different. In particular, an alternative copper transport system Cus is present instead of Cop and a putative zero-valent sulfur acceptor protein gene appears just before TcDH. Moreover, in contrast to the thiocyanate-oxidizing Thioalkalivibrio species, both genomes of the halophilic SOB contained a gene encoding the enzyme cyanate hydratase. The sulfur-oxidizing pathway in the genome of Thiohalobacter includes a Fcc type of sulfide dehydrogenase, a rDsr complex/AprAB/Sat for oxidation of zero-valent sulfur to sulfate, and an incomplete Sox pathway, lacking SoxCD. The sulfur oxidation pathway reconstructed from the genome of Guyparkeria sp. SCN-R1 was more similar to that of members of the Thiomicrospira-Hydrogenovibrio group, including a Fcc type of sulfide dehydrogenase and a complete Sox complex. One of the outstanding properties of Thiohalobacter is the presence of a Na+-dependent ATP synthase, which is rarely found in aerobic Prokaryotes.Overall, the results showed that, despite an obvious difference in the general sulfur-oxidation pathways, halophilic and haloalkaliphilic SOB belonging to different genera within the Gammaproteobacteria developed a similar unique thiocyanate-degrading mechanism based on the direct oxidative attack on the sulfane atom of thiocyanate.

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Cyanate (CNO−) has been produced in the environment through either natural or anthropogenic sources. However, due to industrialization, it has been led more over-loads. In this study, interaction of CNO− uptake by rice seedlings with nitrate assimilation was investigated using gene expression analysis after an acute phytotoxicity assay. Our results showed that CNO− exposure caused inhibition on relative growth rates of plants. CNO− analysis demonstrated that rice seedlings had higher potential for CNO− uptake and the removal rates showed a zero-order kinetic. PCR analysis exposed that OsCYN transcript was not significantly induced by CNO− treatments in rice tissues and CNO− exposure also repressed gene expression of the collaborative enzyme carbonic anhydrase (CA), suggesting that assimilation of CNO− initiated by the enzyme cyanase (CYN) in rice seedlings was an enzyme-limitation reaction. Gene expression of other enzymes involved in nitrate metabolism was tissue-specific under CNO− exposure, suggesting that rice seedlings were able to trigger its intrinsic regulative and responsive mechanisms to cope up with uneven N conditions. Significant upregulation of three OsGDH isogenes, except for OsGDH1 in roots, was detected in both rice materials with enhancing CNO− concentrations, suggesting that GDH may play a primary role to maintain the balance of C and N in plants under CNO− exposure. In conclusion, because the innate pool of CYN activity was non-sufficient to degrade exogenous CNO− by rice seedlings, CNO-derived ammonium only can serve as a supporting N source to support growth of rice seedling under non-effective doses of CNO− exposure. [ABSTRACT FROM AUTHOR]

Graphical abstract Highlights • The ZnO-B catalyst was synthesized by sol-gel method. • A central composite faced design was used to maximize the cyanide degradation. • The cyanide was almost degraded by ZnO-B under simulated solar light. • The intermediate ions quantified (OCN−, NO 3 − and NH 4 +) indicated a low toxic effluent. • The cyanide degradation process occurred with participation of h+ and OH. Abstract The photocatalytic activity of boron-doped ZnO with varying concentration (1, 1.5 and 2% wt of B) synthesized by sol-gel method was evaluated on cyanide (CN−) degradation in aqueous solution under simulated solar radiation. The obtained catalysts were characterized by XRD, UV–vis/DRS, ICP-OES, FT-IR, and XPS. The photocatalytic experiments were carried out in a quartz batch reactor using 300 mL of cyanide solution adjusted at pH 11, evaluating different parameters such as the amount of B dopant, catalyst loading and initial concentration of cyanide solution. A 23 central composite faced design was used to maximize CN− photocatalytic degradation. The cyanide concentration was measured by ISE potentiometric method and the content of intermediate ions (OCN−, NO 3 −, and NH 4 +) was determined by UV–vis spectrophotometry. The boron incorporation into ZnO lattice (ZnO-B) reduced wurtzite crystallite size (25 nm) and narrowed the band gap (3.0 eV) compared to bare ZnO (43 nm and 3.2 eV, respectively). The ZnO-B 1.5 wt% showed better photocatalytic performance by degrading 89% of a 10 mg L-1 CN− solution compared to 75% that was reached by undoped ZnO; using in both cases 1.4 g L-1 of catalyst loading at accumulated energy of 400 kJ m-2. [ABSTRACT FROM AUTHOR]

The genomes of Thiohalobacter thiocyanaticus and Guyparkeria (formerly known as Halothiobacillus) sp. SCN-R1, two gammaproteobacterial halophilic sulfur-oxidizing bacteria (SOB) capable of thiocyanate oxidation via the "cyanate pathway", have been analyzed with a particular focus on their thiocyanate-oxidizing potential and sulfur oxidation pathways. Both genomes encode homologs of the enzyme thiocyanate dehydrogenase (TcDH) that oxidizes thiocyanate via the "cyanate pathway" in members of the haloalkaliphilic SOB of the genus Thioalkalivibrio. However, despite the presence of conservative motives indicative of TcDH, the putative TcDH of the halophilic SOB have a low overall amino acid similarity to the Thioalkalivibrio enzyme, and also the surrounding genes in the TcDH locus were different. In particular, an alternative copper transport system Cus is present instead of Cop and a putative zero-valent sulfur acceptor protein gene appears just before TcDH. Moreover, in contrast to the thiocyanate-oxidizing Thioalkalivibrio species, both genomes of the halophilic SOB contained a gene encoding the enzyme cyanate hydratase. The sulfur-oxidizing pathway in the genome of Thiohalobacter includes a Fcc type of sulfide dehydrogenase, a rDsr complex/AprAB/Sat for oxidation of zero-valent sulfur to sulfate, and an incomplete Sox pathway, lacking SoxCD. The sulfur oxidation pathway reconstructed from the genome of Guyparkeria sp. SCN-R1 was more similar to that of members of the Thiomicrospira-Hydrogenovibrio group, including a Fcc type of sulfide dehydrogenase and a complete Sox complex. One of the outstanding properties of Thiohalobacter is the presence of a Na+-dependent ATP synthase, which is rarely found in aerobic Prokaryotes.Overall, the results showed that, despite an obvious difference in the general sulfur-oxidation pathways, halophilic and haloalkaliphilic SOB belonging to different genera within the Gammaproteobacteria developed a similar unique thiocyanate-degrading mechanism based on the direct oxidative attack on the sulfane atom of thiocyanate. [ABSTRACT FROM AUTHOR]

Graphical abstract Highlights • First report on the immobilization of rTl-Cyn onto magnetic-multiwall carbon nanotubes. • First report on the simultaneous removal of cyanate and heavy metals from a wastewater sample. • Immobilized enzyme displayed >94% of initial activity after ten cycles. Abstract Global environmental problems allied with waste management require novel approaches for the simultaneous removal of heavy metals and other associated compounds including cyanate. In this study, iron-oxide filled multi-walled carbon nanotubes (m-MWCNTs) were successfully synthesized and characterized by field emission gun scanning electron microscopy (FEGSEM), high-resolution transmission electron microscopy (HRTEM) and X-ray diffraction (XRD). The m-MWCNTs were amino-functionalized for the covalent immobilization of a recombinant cyanate hydratase (rTl-Cyn), and were characterized by fourier transform infrared (FTIR) spectroscopy. The immobilized rTl-Cyn on the m-MWCNTs (m-MWCNT-rTl-Cyn) had long term storage stability and showed great potential towards cyanate biodegradability. We found that m-MWCNT-rTl-Cyn retained >94% of the initial activity even after 10 repeated cycles of bio-catalysis. Strikingly, the m-MWCNT-rTl-Cyn simultaneously reduced the concentration of chromium (Cr), iron (Fe), lead (Pb) and copper (Cu) by 39.31, 35.53, 34.48 and 29.63%, respectively as well as the concentration of cyanate by ≥84%, in a synthetic wastewater sample. [ABSTRACT FROM AUTHOR]

Ammonia-oxidizing archaea (AOA) and bacteria (AOB), nitrite-oxidizing bacteria (NOB), and complete ammonia oxidizers (comammox) are responsible for nitrification in nature; however, some groups have been reported to utilize labile-dissolved organic nitrogen (LDON) for satisfying nitrogen demands. To understand the universality of their capacity of LDON metabolism, we collected 70 complete genomes of AOA, AOB, NOB, and comammox from typical environments for exploring their potentials in the metabolism of representative LDON (urea, polyamines, cyanate, taurine, glycine betaine, and methylamine). Genomic analyses showed that urea was the most popular LDON used by nitrifiers. Each group harbored unique urea transporter genes (AOA: dur3 and utp , AOB: utp , and NOB and comammox: urtABCDE and utp ) accompanied by urease genes ureABC . The differentiation in the substrate affinity of these transporters implied the divergence of urea utilization efficiency in nitrifiers, potentially driving them into different niches. The cyanate transporter ( cynABD and focA/nirC ) and degradation ( cynS ) genes were detected mostly in NOB, indicating their preference for a wide range of nitrogen substrates to satisfy high nitrogen demands. The lack of genes involved in the metabolism of polyamines, taurine, glycine betaine, and methylamines in most of nitrifiers suggested that they were not able to serve as a source of ammonium, only if they were degraded or oxidized extracellularly as previously reported. The phylogenetic analyses assisted with comparisons of GC% and the Codon Adaptation Index between target genes and whole genomes of nitrifiers implied that urea metabolic genes dur3 and ureC in AOA evolved independently from bacteria during the transition from Thaumarchaeota to AOA, while utp in terrestrial AOA was acquired from bacteria via lateral gene transfer (LGT). Cyanate transporter genes cynS and focA / nirC detected only in a terrestrial AOA Candidadus Nitrsosphaera gargensis Ga9.2 could be gained synchronously with Nitrospira of NOB by an ancient LGT. Our results indicated that LDON utilization was a common feature in nitrifiers, but metabolic potentials were different among nitrifiers, possibly being intensely interacted with their niches, survival strategies, and evolutions., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2023 Liu, Chen and Xu.)

Abstract Rationale Cystic fibrosis (CF) patients are known to produce cyanide (CN-) although challenges exist in determinations of total levels, the precise bioactive levels, and specificity of its production by CF microflora, especially P. aeruginosa. Our objective was to measure total CN- levels in CF sputa by a simple and novel technique in P. aeruginosa positive and negative adult patients, to review respiratory tract (RT) mechanisms for the production and degradation of CN-, and to interrogate sputa for post-translational protein modification by CN- metabolites. Methods Sputa CN- concentrations were determined by using a commercially available CN- electrode, measuring levels before and after addition of cobinamide, a compound with extremely high affinity for CN-. Detection of protein carbamoylation was measured by Western blot. Measurements and main results The commercial CN- electrode was found to overestimate CN- levels in CF sputum in a highly variable manner; cobinamide addition rectified this analytical issue. Although P. aeruginosa positive patients tended to have higher total CN- values, no significant differences in CN- levels were found between positive and negative sputa. The inflammatory oxidant hypochlorous acid (HOCl) was shown to rapidly decompose CN-, forming cyanogen chloride (CNCl) and the carbamoylating species cyanate (NCO-). Carbamoylated proteins were found in CF sputa, analogous to reported findings in asthma. Conclusions Our studies indicate that CN- is a transient species in the inflamed CF airway due to multiple biosynthetic and metabolic processes. Stable metabolites of CN-, such as cyanate, or carbamoylated proteins, may be suitable biomarkers of overall CN- production in CF airways. Graphical abstract fx1 Highlights • Ion-specific electrode and cobinamide used to quantify CN- in CF sputum. • Sputum CN - levels do not correlate with infection or lung function. • Hypochlorous acid rapidly degrades CN- into cyanogen chloride and cyanate. • CF respiratory tract biosynthetic and catabolic pathways of CN- reviewed. • Carbomoylated proteins are present in CF sputum. [ABSTRACT FROM AUTHOR]

Abstract: A general synthetic protocol for the synthesis of phosphorus‐ and arsenic‐containing analogues of the thio‐ and seleno‐cyanate anions is reported. This procedure allows for the isolation of three unprecedented species: the phosphaethynselenolate, PCSe− (1), the arsaethynthiolate, AsCS− (2), and the arsaethynselenolate, AsCSe− (3), anions. The structures, electronic properties, and spectroscopic signatures of these species are reported. [ABSTRACT FROM AUTHOR]

Degradation of urea in 8 mol·L−1 aqueous solution (20% w/w N) has been studied at 298.15 ± 0.01 K over a time period of 150 days. The data were obtained by periodicaly measuring the electric conductivity, acidity, and concentrations of the main species of the solution, such as cyanate, ammonim carbonate and ammonium hydrogencarbonate. The concentration of un-ionized ammonia was calculated on the basis of the data for the total ammonia content in the solution. [ABSTRACT FROM AUTHOR]

Abstract: Carbamylation (or carbamoylation) is a non‐enzymatic modification of biomolecules mediated by cyanate, a dissociation product of urea. Proteins are more sensitive to carbamylation. Two major sites of carbamylation reaction are: Nα‐amino moiety of a protein N‐terminus and the Nɛ‐amino moiety of proteins’ lysine residues. In kidney diseases, urea accumulates and the burden of carbamylation increases. This may lead to alteration in the structure and function of many important proteins relevant in maintenance of homeostasis. Carbamylated proteins namely, carbamylated‐haemoglobin and carbamylated‐low density lipoprotein (LDL) have been implicated in hypoxia and atherosclerosis, respectively. Furthermore, carbamylation of insulin, oxytocin, and erythropoietin have caused changes in the action of these hormones vis‐à‐vis the metabolic pathways they control. In this short review, authors have compiled the data on role of carbamylated proteins, enzymes, hormones, LDL, and so on, in human diseases. © 2018 IUBMB Life, 70(4):267–275, 2018 [ABSTRACT FROM AUTHOR]

Cyanase detoxifies cyanate by transforming it to ammonia and carbon dioxide in a bicarbonate-dependent reaction, however, dependence on bicarbonate limits its utilization in large-scale applications. A novel strategy was therefore developed for overcoming this bottleneck by the combined application of cyanase (rTl-Cyn) and carbonic anhydrase (rTl-CA). The synergistic effect of rTl-Cyn and rTl-CA could reduce the dependence of bicarbonate by 80%, compared to using rTl-Cyn alone. Complete degradation of cyanate (4 mM) was achieved with buffered conditions and 85 ± 5% degradation with industrial wastewater sample, when 20 U of rTl-Cyn was applied. Furthermore, a similar percentage of degradation was achieved using 80% less bicarbonate, when rTl-Cyn and rTl-CA were used together under identical conditions. In addition, rTl-Cyn and rTl-CA were immobilized onto the magnetic nanoparticles and their catalytic activity, stability and reusability were also evaluated. This is the first report on the synergistic biocatalysis by rTl-Cyn and rTl-CA, for cyanate detoxification. [ABSTRACT FROM AUTHOR]

Mining, jewellery and metal-processing industries use cyanide for extracting gold and other valuable metals, generating large amounts of highly toxic wastewater. Biological treatments may be a clean alternative under the environmental point of view to the conventional physical or chemical processes used to remove cyanide and related compounds from these industrial effluents. Pseudomonas pseudoalcaligenes CECT5344 can grow under alkaline conditions using cyanide, cyanate or different nitriles as the sole nitrogen source, and is able to remove up to 12 mM total cyanide from a jewellery industry wastewater that contains cyanide free and complexed to metals. Complete genome sequencing of this bacterium has allowed the application of transcriptomic and proteomic techniques, providing a holistic view of the cyanide biodegradation process. The complex response to cyanide by the cyanotrophic bacterium P. pseudoalcaligenes CECT5344 and the potential biotechnological applications of this model organism in the bioremediation of cyanide-containing industrial residues are reviewed. [ABSTRACT FROM AUTHOR]

Obesity is an important contributing factor to progression of chronic kidney disease. Cyanate, known as uremic toxin, is an electrophile produced spontaneously from urea or by myeloperoxidase-catalyzed oxidation of thiocyanate. Herein, we explored metabolic effects of cyanate in normal chow diet (NCD)- and high fat diet (HFD)-fed mice. Mice were treated with cyanate (1 mg/mL in drinking water) and fed NCD or HFD. Peritoneal glucose tolerance test (PGTT) and insulin tolerance test (ITT) were performed. Blood urea nitrogen (BUN) and creatinine concentrations were determined. Kidney and liver tissues were analyzed for reactive oxygen species (ROS) and lipid accumulations. Human albumin was carbamylated and evaluated for ROS scavenging activities. Contrary to our expectations, we found that cyanate treatment improved increased insulin sensitivity and alleviated hepatic steatosis in NCD- and HFD-fed mice. PGTT and ITT revealed faster and immediate glucose clearance in cyanate-treated NCD- and HFD-fed mice. Histological analysis of kidney and serum levels of BUN and creatinine showed no significant differences between cyanate-treated and control mice groups. Cyanate treatment reduced appetite and body weight in both NCD- and HFD-fed mice groups. Cyanate also decreased lipid peroxidation levels in the sera and the kidney, attenuated ROS levels in the kidney, which lead us to the findings that cAlb significantly reduced ROS levels compared to Alb in Caki-1 kidney and human umbilical vein endothelial cells. The results in this study may indicate that cyanate improves insulin sensitivity and hepatic steatosis possibly via exerting anorexic and antioxidative effects. [ABSTRACT FROM AUTHOR]

Urea, a marker of uraemic retention in chronic kidney disease (CKD) and of adequacy of intradialytic solute removal, has traditionally been considered to be biologically inert. However, a number of recent experimental data suggest that urea is toxic at concentrations representative for CKD. First of all, at least five studies indicate that urea itself induces molecular changes related to insulin resistance, free radical production, apoptosis and disruption of the protective intestinal barrier. Second, urea is at the origin of the generation of cyanate, ammonia and carbamylated compounds, which as such all have been linked to biological changes. Especially carbamylation has been held responsible for post-translational protein modifications that are involved in atherogenesis and other functional changes. In observational clinical studies, these carbamylated compounds were associated with cardiovascular and overall morbidity and mortality. These findings shed new light on the validity of Kt/Vurea as a marker of dialysis adequacy. Yet, also the views that the kinetics of urea are not representative of the kinetics of several other uraemic retention solutes, and that urea cannot be held responsible for all complex metabolic and clinical changes responsible for the uraemic syndrome, still remain valid. Future efforts to improve the outcome of patients with CKD might be directed at further improving removal of solutes implied in the uraemic syndrome, including but not restricted to urea, also taking into account the impact of the intestine and (residual) renal function on solute concentration. [ABSTRACT FROM AUTHOR]

Chronic kidney disease (CKD) is problem that has become one of the major issues affecting public health. Extensive clinical data suggests that the prevalence of hyperlipidemia in CKD patients is significantly higher than in the general population. Lipid metabolism disorders can damage the renal parenchyma and promote the occurrence of cardiovascular disease (CVD). Cyanate is a uremic toxin that has attracted widespread attention in recent years. Usually, 0.8% of the molar concentration of urea is converted into cyanate, while myeloperoxidase (MPO) catalyzes the oxidation of thiocyanate to produce cyanate at the site of inflammation during smoking, inflammation, or exposure to environmental pollution. One of the important physiological functions of cyanate is protein carbonylation, a non-enzymatic post-translational protein modification. Carbamylation reactions on proteins are capable of irreversibly changing protein structure and function, resulting in pathologic molecular and cellular responses. In addition, recent studies have shown that cyanate can directly damage vascular tissue by producing large amounts of reactive oxygen species (ROS). Oxidative stress leads to the disorder of liver lipid metabolism, which is also an important mechanism leading to cirrhosis and liver fibrosis. However, the influence of cyanate on liver has remained unclear. In this research, we explored the effects of cyanate on the oxidative stress injury and abnormal lipid metabolism in mice and HL-7702 cells. In results, cyanate induced hyperlipidemia and oxidative stress by influencing the content of total cholesterol (TC), high-density lipoprotein (HDL), low-density lipoprotein (LDL), superoxide dismutase (SOD), catalase (CAT) in liver. Cyanate inhibited NF-E2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1), and the phosphorylation of adenosine 5′monophosphate-activated protein kinase (AMPK), activated the mTOR pathway. Oxidative stress on the cells reduced significantly by treating with TBHQ, an antioxidant, which is also an activator of Nrf2. The activity of Nrf2 was rehabilitated and phosphorylation of mTOR decreased. In conclusion, cyanate could induce oxidative stress damage and lipid deposition by inhibiting Nrf2/HO-1 pathway, which was rescued by inhibitor of Nrf2.