Academic literature on the topic 'Mixed function oxygenases'

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Journal articles on the topic "Mixed function oxygenases"

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Rattner, Barnett A., David J. Hoffman, and Carolyn M. Marn. "Use of mixed-function oxygenases to monitor contaminant exposure in wildlife." Environmental Toxicology and Chemistry 8, no. 12 (1989): 1093–102. http://dx.doi.org/10.1002/etc.5620081202.

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Zahn, R. K., J. J. Stüber, M. Reitz, C. Emmig, U. Jannek, and B. Kurelec. "The interplay between mixed function oxygenases and DNA alteration under PAH pollution." Marine Environmental Research 17, no. 2-4 (1985): 317–19. http://dx.doi.org/10.1016/0141-1136(85)90123-0.

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Dürk, H., J. L. Poyer, C. Klessen, and H. Frank. "Acetylene, a mammalian metabolite of 1,1,1-trichloroethane." Biochemical Journal 286, no. 2 (1992): 353–56. http://dx.doi.org/10.1042/bj2860353.

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1,1,1-Trichloroethane (TCE) is a widely used industrial solvent of low acute toxicity. It is slowly oxidized to trichloroethanol and trichloroacetic acid by cytochrome P-450-dependent mono-oxygenases. Increased inhalative uptake by rats under hypoxia and spin-trapping experiments indicate that TCE is also reductively metabolized to a radical intermediate. Acetylene is formed as a metabolite, suggesting transfer of an additional electron to form the corresponding carbene. Hypoxia and induction of mixed-function mono-oxygenases accelerate the formation of acetylene. Experiments performed in vitro with rat liver microsomal fractions yield analogous results.
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Ferreira, Rui, Fátima Candeias, Fátima Simões, José Nascimento, and J. Cruz Morais. "Effects of horminone on liver mixed function mono-oxygenases and glutathione enzyme activities of Wistar Rat." Journal of Ethnopharmacology 58, no. 1 (1997): 21–30. http://dx.doi.org/10.1016/s0378-8741(97)00073-1.

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Custer, T. W., C. M. Custer, R. K. Hines, et al. "Mixed-Function Oxygenases, Oxidative Stress, and Chromosomal Damage Measured in Lesser Scaup Wintering on the Indiana Harbor Canal." Archives of Environmental Contamination and Toxicology 38, no. 4 (2000): 522–29. http://dx.doi.org/10.1007/s002449910068.

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Geisler, J., B. A. Engelsen, H. Berntsen, S. Geisler, and P. E. Lønning. "Differential effect of carbamazepine and valproate monotherapy on plasma levels of oestrone sulphate and dehydroepiandrosterone sulphate in male epileptic patients." Journal of Endocrinology 153, no. 2 (1997): 307–12. http://dx.doi.org/10.1677/joe.0.1530307.

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Abstract Steroid sulphates such as oestrone sulphate (OE1S) and dehydroepiandrosterone sulphate (DHEAS) have been suggested to be of biological importance in different disease states such as breast cancer and atherosclerosis. Previous studies have shown that drugs such as aminoglutethimide and rifampicin that induce P450-dependent mixed-function oxygenases selectively suppress plasma OE1S levels. The aim of this study was to evaluate the influence of treatment with carbamazepine, an antiepileptic drug known to stimulate mixed-function oxygenases, on plasma levels of OE1S and DHEAS. We measured plasma OE1S and DHEAS together with other plasma oestrogens and androgens in male epileptic patients before and during carbamazepine monotherapy. Patients treated with valproate monotherapy acted as a control group. Treatment with carbamazepine decreased plasma OE1S levels from a mean value of 810·8 to 411·6 pmol/l (mean suppression to 50·7% of pretreatment levels, P<0·001). Similarly, the ratio of OE1S to OE1 fell to 59·9% of pretreatment levels (P<0·001). DHEAS decreased from a mean level of 4·9 μmol/l before treatment to 3·0 μmol/l during carbamazepine therapy (mean reduction to 62·7% of pretreatment levels (P<0·001)), while the ratio of DHEAS to DHEA fell to 63·0% of pretreatment values (P<0·01). No significant change in plasma levels of the other oestrogens or androgens measured was observed. Treatment with valproate caused a slight decrease in FSH levels (P<0·05), but no change in any of the other hormones measured was observed. Studies are warranted to evaluate the possible effects of long-term treatment with carbamazepine on the risk of developing endocrine-sensitive tumours and cardiovascular disease and also the possible effects of alterations in plasma DHEAS on epileptic activity. Journal of Endocrinology (1997) 153, 307–312
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Fowler, Claire A., Glyn R. Hemsworth, Fiona Cuskin, et al. "Structure and function of a glycoside hydrolase family 8 endoxylanase from Teredinibacter turnerae." Acta Crystallographica Section D Structural Biology 74, no. 10 (2018): 946–55. http://dx.doi.org/10.1107/s2059798318009737.

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The biological conversion of lignocellulosic matter into high-value chemicals or biofuels is of increasing industrial importance as the sector slowly transitions away from nonrenewable sources. Many industrial processes involve the use of cellulolytic enzyme cocktails – a selection of glycoside hydrolases and, increasingly, polysaccharide oxygenases – to break down recalcitrant plant polysaccharides. ORFs from the genome of Teredinibacter turnerae, a symbiont hosted within the gills of marine shipworms, were identified in order to search for enzymes with desirable traits. Here, a putative T. turnerae glycoside hydrolase from family 8, hereafter referred to as TtGH8, is analysed. The enzyme is shown to be active against β-1,4-xylan and mixed-linkage (β-1,3,β-1,4) marine xylan. Kinetic parameters, obtained using high-performance anion-exchange chromatography with pulsed amperometric detection and 3,5-dinitrosalicyclic acid reducing-sugar assays, show that TtGH8 catalyses the hydrolysis of β-1,4-xylohexaose with a k cat/K m of 7.5 × 107 M −1 min−1 but displays maximal activity against mixed-linkage polymeric xylans, hinting at a primary role in the degradation of marine polysaccharides. The three-dimensional structure of TtGH8 was solved in uncomplexed and xylobiose-, xylotriose- and xylohexaose-bound forms at approximately 1.5 Å resolution; the latter was consistent with the greater k cat/K m for hexasaccharide substrates. A 2,5 B boat conformation observed in the −1 position of bound xylotriose is consistent with the proposed conformational itinerary for this class of enzyme. This work shows TtGH8 to be effective at the degradation of xylan-based substrates, notably marine xylan, further exemplifying the potential of T. turnerae for effective and diverse biomass degradation.
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Payne, Jerry F., L. Fancey, J. Kiceniuk, U. Williams, Jim Osborne, and Anver Rahimtula. "Mixed-function oxygenases as biological monitors around petroleum hydrocarbon development sites: Potential for induction by diesel and other drilling mud base oils containing reduced levels of polycyclic aromatic hydrocarbons." Marine Environmental Research 17, no. 2-4 (1985): 328–32. http://dx.doi.org/10.1016/0141-1136(85)90126-6.

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Clausen, Jørgen, and Søren Achim Nielsen. "A Sensitive Method for Assay of Mixed-Function Oxygenase (p-450 complex) in Cell Culture." Alternatives to Laboratory Animals 15, no. 3 (1988): 219–23. http://dx.doi.org/10.1177/026119298801500310.

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The mixed-function oxygenase system involved in the metabolism of drugs and xenobiotics has been extensively studied in various animal species and in various organs (1). It is now apparent that in humans the p-450 complex is one representative of a related family, expressed by 13 c-DNA genes showing approximately 36% similarity between the different subfamilies (2). In order to compare the in vivo and in vitro metabolic effects of drugs and xenobiotics, the induction capabilities of the mixed-function oxygenase must be known. The most sensitive non-isotopic assay system for determination of mixed-function oxygenase activity is the method of Nebert & Gelboin (3,4), which is based on the metabolic transformation of benzo-(a)-pyrene to its fluorescent hydroxyl derivatives (5). However, the levels of the mixed-function oxygenase enzymes in different cellular systems show great variations, with the highest activities in liver cells. Therefore, in order to use human lymphocytes and other cellular systems with low mixed-function oxygenase activities, the assay method for determining oxygenase activity must have the highest possible sensitivity. The present communication is devoted to a study aimed at increasing the sensitivity of Nebert & Gelboin's methods for assay of mixed-function oxygenase subfamilies using benzo-(a)-pyrene as a substrate.
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Rocha-e-Silva, Thomaz A. A., Marcelo M. Rossa, Francisco T. Rantin, Takako Matsumura-Tundisi, Jose G. Tundisi, and Igor A. Degterev. "Comparison of liver mixed-function oxygenase and antioxidant enzymes in vertebrates." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 137, no. 2 (2004): 155–65. http://dx.doi.org/10.1016/j.cca.2004.01.007.

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Dissertations / Theses on the topic "Mixed function oxygenases"

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Ekström, Fredrik. "X-ray characterization of PaPheOH, a bacterial phenylalanine hydroxylase /." Umeå : Univ, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-100.

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Harrelson, John P. "A comparative study of cytochromes P450 2E1 and 2A6 : substrate dynamics, multiple ligand binding, and adduct formatioin by N-acetyl-m-aminophenol /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/8166.

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Meckley, Lisa M. "Clinical utility, cost-effectiveness and provider perceptions of CYP2C9 and VKORC1 genotyping for chronic warfarin therapy /." Thesis, Connect to this title online; UW restricted, 2008. http://hdl.handle.net/1773/7960.

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Karlgren, Maria. "Novel extrahepatic P450 enzymes with emphasis on the tumor specific CYP2W1 /." Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-139-5/.

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Limdi, Nita A. "Influence of CYP2C9 and VKORC1 genotypes on warfarin response in African-American and European American patients." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2009r/limdi.pdf.

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Mathieu, Delphine. "Etude de systèmes modèles des enzymes à fer utilisant la tetrahydrobiopterine comme cofacteur, les no synthases et les hydroxylases d'acides aminés aromatiques." Paris 5, 2004. http://www.theses.fr/2004PA05P601.

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La tétrahydrobioptérine (H4B) intervient comme cofacteur de deux familles d'enzymes importantes chez les mammifères, les NO synthases (NOS) et les hydroxylases d'acides aminés aromatiques (HAAA). Afin de mieux comprendre le rôle de H4B dans ces enzymes et les spécificités apportées par ce cofacteur, nous avons étudié des systèmes chimiques modèles faisant intervenir H4B ou d'autres tetrahydroptérines (H4P). Nous avons montré que, de façon très générale, les tétrahydroptérines transfèrent un électron aux porphyrines de fer, dans l'état FeIII ou FeIIO2, avec formation du radical cation (H4P)+· correspondant. Ceci nous a conduit au premier modèle chimique de la réaction de transfert d'électron intervenant dans la NOS. Au cours de l'étude de systèmes modèles des HAAA, nous avons mis en évidence une régiosélectivité originale favorisant l'hydroxylation aromatique en position méta, lorsque le réducteur utilisé est une tétrahydroptérine ou l'ascorbate<br>Tetrahydrobiopterin (H4B) is a cofactor for two important families of mammals' enzymes, the NO synthases (NOS) and the aromatic amino acid hydroxylases (AAAH). To better understand the role of H4B in these enzymes and the specificities linked to this cofactor, we studied chemical model systems using H4B or other tetrahydropterins (H4P). We showed, in a very general manner, that tetrahydropterins transfer an electron to iron porphyrins, either in their FeIII or FeIIO2 state, with formation of the corresponding cation radical (H4P)+·. This led us to the first chemical model for the electron transfer reaction happening in NOS. While studying AAAH model systems, we highlighted a surprising regioselectivity in favour of aromatic hydroxylation in the meta position, when the reductant used is either a tetrahydropterin or ascorbate
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Dalgard, Clifton Lee. "Hypoxia-inducible factor hydroxylases are oxygen sensors in the brain /." Download the dissertation in PDF, 2005. http://www.lrc.usuhs.mil/dissertations/pdf/Dalgard2005.pdf.

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Tugiyono. "Metabolic enzymes and mixed-function oxygenase (MFO) system in pink snapper (Pagrus auratus) : biochemical and histological relationships /." Curtin University of Technology, Department of Environmental Biology, 2001. http://espace.library.curtin.edu.au:80/R/?func=dbin-jump-full&object_id=13744.

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The environmental health of aquatic ecosystems depends amongst others, on the chemical pollution coming from activities in the catchment's area. In the Swan River Estuary, Western Australia, the chemical pollutants of concern released into the river are petroleum hydrocarbons and sodium pentachlorophenate (NaPCP). Decreased water quality causes a loss of biotic diversity especially amongst fish populations. The health of aquatic ecosystems can be monitored by fish health, especially fish located at higher levels in the food chain. Pink snapper (Pagrus auratus), an endemic Western Australian fish species, was tested for its potential as a bioindicator of aquatic environmental health. This thesis presents data on the responsiveness of pink snapper to the contaminants of concern, using biomarkers such as serum sorbitol dehydrogenase (SDH), mixed function oxygenase (MFO), metabolic enzymes such as citrate synthase (CS), cytochrome C oxidase (CCO) and lactate dehydrogenase (LDH) and the histological alteration such as hepatic cell lesions (hyperplasia and hypertrophy), and glycogen and lipid droplets. The metabolic enzymes CCO and LDH as well as the hepatic MFO induction and histopathology were proven to be the most suitable biomarkers for use for routine monitoring of the Swan River Estuary using pink snapper as a bioindicator. However, CS activity and hepatic cell lesions (hyperplasia and hypertrophy) did not respond to exposure to contamination and are therefore not suited as biomarkers of effects in pink snapper. The first phase of the study aimed at investigating the responsiveness of juvenile pink snapper to an MFO inducer. Polychlorinated biphenyl isomer # 126 was selected as a model MFO inducer for this study. In the initial experiment, MFO activity was measured as a biomarker of exposure, and serum SDH activity was assessed as a biomarker of liver damage.<br>MFO and SDH activities were of special interest as these biochemical tools have not previously been validated for any Western Australia fish species. Juvenile pink snapper were injected intraperitoneally (i.p.) with 0, 10, 100, 500, 1000 microgram PCB-126 per kilogram. Fish were sacrificed 10 days postinjection, and liver and blood were collected for MFO and SDH analysis, respectively. Doses of 10 and 100 microgram PCB-126 per kilogram caused the highest MFO induction, while doses of 0 and 1000 microgram PCB-126 per kilogram did not result in higher MFO activity relative to carrier-injected (peanut oil) control fish. SDH activities were not significantly different among treatments indicating that hepatocellular damage was not responsible for the reduced MFO activity at the highest dose. Metabolic enzymes in pink snapper exposed by NaPCP were studied in the second phase of the experiment. The aim of this second experiment was to test the responsiveness of pink snapper to contaminants known to cause metabolic perturbations in vertebrates. Juvenile pink snapper were intraperitoneally (i.p.) injected with 0, 5, 10, 20 mg per kilogram. Oxidative enzymes were assessed by measuring CS and CCO activities and glycolytic enzyme was assessed by measuring LDI-1 activity in liver and white muscle tissues. CS activity remained unchanged in both the white muscle and in the liver. CCO activity was significantly enhanced in liver in all treated fish relative to control fish, but not in the white muscle. LDH activity was also higher in liver in all treated fish as compared to control fish, while in white muscle, LDH activity significantly increased at the highest dose injected.<br>The use of a suite of biochemical markers is useful in determining the effects of xenobiotic exposure of aquatic organisms, because it provides a holistic approach with biomarkers at different levels of biological organization. For the third and final phase of the study the suite of biomarkers selected were MFO, metabolic enzyme (CS, CCO and LDH) activities, and histological alternations in combination with physiological indices. The aim of this last experiment was to investigate if a modified liver metabolic activity would alter the MFO induction potential. To test if altered liver metabolism would influence liver detoxication capacities, juvenile pink snapper were i.p. injected with peanut oil (control), or pentachlorobiphenyl # 126 (PCB 126), with sodium pentachlorophenate (NaPCP), or combination of PCB 126+NaPCP. Relative to controls, ethoxyresorufin-O-deethylase (EROD) activity was induced in the PCB 126 and PCB 126+NaPCP fish, but not in the NaPCP group. In the liver, CCO activity was enhanced by the treatments while CS activity remained unchanged and LDH activity was increased in the NaPCP treatment only. In the white muscle, only the PCB 126+ NaPCP treatment enhanced CCO activity, with all other enzymatic activities remaining unchanged. Low serum sorbitol dehydrogenase (sSDH) activity and histopathology of the liver indicated no significant alteration of cellular structure, albeit the lipid droplet size was increased in the PCB 126 and in the PCB 126+NaPCP treatments.<br>It is concluded that the hepatic metabolic changes correspond to histopathological observations, but an altered metabolic capacity does not influence the metabolism of xenobiotics by liver enzymes, as measured by EROD activity. These experiments answered the need to identify a suitable fish species for routine monitoring of the aquatic environment in Western Australia. It also identified the most suitable biochemical markers of exposure and effects, and the suitability of the pink snapper as a bioindicator. Finally, the experiments investigated interactions between biomarkers and provided new knowledge useful to scientists using MFO and/or metabolic enzymes in field or laboratory toxicology.
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Fragoso, Nuno M. "Mixed-function oxygenase activity of rainbow trout (Oncorhynchus mykiss) in relation to exposure, accumulation and elimination of retene." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape17/PQDD_0014/MQ31205.pdf.

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Osman, Abdimajid. "Studies on warfarin treatment with emphasis on inter-individual variations and drug monitoring." Doctoral thesis, Linköping : Linköping University, 2007. http://www.bibl.liu.se/liupubl/disp/disp2007/med1000s.pdf.

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Books on the topic "Mixed function oxygenases"

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Canada. Dept. of Fisheries and Oceans. Physical and Chemical Sciences Branch. Protocols for measuring mixed function oxygenases of fish liver. Physical and Chemical Sciences Branch, Dept. of Fisheries and Oceans, 1991.

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Lockhart, W. L. Analysis for liver mixed function oxygenase in fish, Peace, Athabasca and Slave River Basins, September to December, 1994. Northern River Basins Study, 1996.

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Branch, Canada Dept of Fisheries and Oceans Science. Biomarkers of stress in urban rivers: Mixed-function-oxygenase and acetylcholinesterase effects in brown trout in rivers in St.John's, Newfoundland. Science Branch, Dept. of Fisheries and Oceans, 1994.

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Parrott, Joanne Louise. Accumulation of fish mixed function oxygenase inducers by semipermeable membrane devices in river water and effluents, Athabasca, Peace and Wapiti rivers, August and September, 1995. The Study, 1996.

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1942-, Schmid Rolf, and Urlacher Vlada B, eds. Modern biooxidation: Enzymes, reactions, and applications. Wiley-VCH, 2007.

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Modern biooxidation: Enzymes, reactions and applications. Wiley-VCH, 2008.

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Accumulation of fish mixed function oxygenase inducers by semipermeable membrane devices in river water and effluents, Athabasca River, August and September, 1994. Northern River Basins Study, 1996.

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Book chapters on the topic "Mixed function oxygenases"

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Korsloot, André, Cornelis A. M. van Gestel, and Nico M. van Straalen. "The mixed-function oxygenase system." In Environmental Stress and Cellular Response in Arthropods. CRC Press, 2004. http://dx.doi.org/10.1201/9781420023336-6.

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"The mixed-function oxygenase system." In Environmental Stress and Cellular Response in Arthropods. CRC Press, 2004. http://dx.doi.org/10.1201/9781420023336.ch6.

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Hodson, Peter V. "Mixed Function Oxygenase Induction by Pulp Mill Effluents: Advances Since 1991." In ENVIRONMENTAL FATE and EFFECTS of PULP and PAPER MILL EFFLUENTS. CRC Press, 2020. http://dx.doi.org/10.1201/9780367812690-35.

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Lee, R., and L. Quattrochi. "Cytochrome P-450 and Mixed-Function Oxygenase Systems in Marine Invertebrates." In Pollutant Studies in Marine Animals. CRC Press, 2018. http://dx.doi.org/10.1201/9781351075831-3.

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Hewitt, L. Mark, John H. Carey, D. George Dixon, and Kelly R. Munkittrick. "Examination of Bleached Kraft Mill Effluent Fractions for Potential Inducers of Mixed Function Oxygenase Activity in Rainbow Trout." In ENVIRONMENTAL FATE and EFFECTS of PULP and PAPER MILL EFFLUENTS. CRC Press, 2020. http://dx.doi.org/10.1201/9780367812690-8.

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Williams, Todd G., John H. Carey, B. Kent Burnison, D. George Dixon, and Hing-Biu Lee. "Rainbow Trout (Oncorhynchus Mykiss) Mixed Function Oxygenase Responses Caused by Unbleached and Bleached Pulp Mill Effluents: A Laboratory-Based Study." In ENVIRONMENTAL FATE and EFFECTS of PULP and PAPER MILL EFFLUENTS. CRC Press, 2020. http://dx.doi.org/10.1201/9780367812690-38.

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Martel, P. H., T. G. Kovacs, and R. H. Voss. "Effluents from Canadian Pulp and Paper Mills: A Recent Investigation of Their Potential to Induce Mixed Function Oxygenase Activity in Fish." In ENVIRONMENTAL FATE and EFFECTS of PULP and PAPER MILL EFFLUENTS. CRC Press, 2020. http://dx.doi.org/10.1201/9780367812690-40.

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Jolivet, Jean-Pierre. "Iron Oxides: An Example of Structural Versatility." In Metal Oxide Nanostructures Chemistry. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780190928117.003.0010.

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Iron is Earth’s fourth most widespread element (6.2% in mass), behind oxygen, silicon, and aluminum. It exists mostly as ferric oxide and oxyhydroxide (Fig. 7.1a) and to a lesser extent as sulfide (pyrite), carbonate (siderite), and silicate (fayalite). Iron oxides are largely used in technological areas such as metallurgy, colored pigments, magnetic materials, and catalysts. They also play an important role in the environment because the dissolution of ferric oxides in natural waters, promoted by acid–base, redox, photochemical phenomena, and also microbial mediation, allows iron to be involved in many biogeochemical processes. Iron is present in many living organisms such as plants, bacteria, mollusks, animals, and humans in various forms: . . . Porphyrinic complexes of iron, which are active centers of hemoglobin and several ferredoxins involved in biological functions, especially respiration mechanism and photosynthesis. Nanoparticles of amorphous ferric oxyhydroxides in animal and human organisms as ferritin, which allows regulation and storage of iron and in various nanophases present in plants as phytoferritin. Crystalline iron oxy(hydroxi)des produced by biomineralization processes. Goethite, lepidocrocite, and magnetite are the main constituents of radulas and the teeth of mollusks (limpets, chitons). Magnetite nanoparticles produced by magnetotactic bacteria (Fig. 7.1b), as well as by bees and pigeons, are used for purposes of orientation and guiding along the lines of force of the Earth’s magnetic field. Green rusts are also ferric- ferrous compounds belonging to the biogeochemical cycle of iron. . . . The crystal chemistry of iron oxy(hydroxi)des is very rich. The ferric, ferrous, and mixed ferric- ferrous oxygenated compounds correspond to around a dozen crystal structural types (Fig. 7.2). Most of these crystal phases can be synthesized from solutions in the laboratory, giving rise to a most diversified chemistry. They are also formed in nature because of the large variability of physicochemical conditions: an acidity range from around pH 0 to 13; redox conditions from oxic to totally anoxic media; bacterial activity that can be extremely intense; salinity largely varying from almost pure waters to real brines; presence of many organic and inorganic ligands; and various photochemical processes.
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