Letteratura scientifica selezionata sul tema "Copper monooxygenases"
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Articoli di riviste sul tema "Copper monooxygenases":
Fukatsu, Arisa, Yuma Morimoto, Hideki Sugimoto e Shinobu Itoh. "Modelling a ‘histidine brace’ motif in mononuclear copper monooxygenases". Chemical Communications 56, n. 38 (2020): 5123–26. http://dx.doi.org/10.1039/d0cc01392g.
Musiani, Francesco, Valquiria Broll, Elisa Evangelisti e Stefano Ciurli. "The model structure of the copper-dependent ammonia monooxygenase". JBIC Journal of Biological Inorganic Chemistry 25, n. 7 (14 settembre 2020): 995–1007. http://dx.doi.org/10.1007/s00775-020-01820-0.
Liew, Elissa F., Daochen Tong, Nicholas V. Coleman e Andrew J. Holmes. "Mutagenesis of the hydrocarbon monooxygenase indicates a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity". Microbiology 160, n. 6 (1 giugno 2014): 1267–77. http://dx.doi.org/10.1099/mic.0.078584-0.
Farhan Ul Haque, Muhammad, Bhagyalakshmi Kalidass, Nathan Bandow, Erick A. Turpin, Alan A. DiSpirito e Jeremy D. Semrau. "Cerium Regulates Expression of Alternative Methanol Dehydrogenases in Methylosinus trichosporium OB3b". Applied and Environmental Microbiology 81, n. 21 (21 agosto 2015): 7546–52. http://dx.doi.org/10.1128/aem.02542-15.
Vu, Van V., e Son Tung Ngo. "Copper active site in polysaccharide monooxygenases". Coordination Chemistry Reviews 368 (agosto 2018): 134–57. http://dx.doi.org/10.1016/j.ccr.2018.04.005.
Blackburn, Ninian J., Brian Reedy, Eilleen Zhou, Robert Carr e Steven J. Benkovic. "Chemistry and spectroscopy of copper monooxygenases". Journal of Inorganic Biochemistry 47, n. 3-4 (luglio 1992): 8. http://dx.doi.org/10.1016/0162-0134(92)84079-3.
Choi, Dong-W., Ryan C. Kunz, Eric S. Boyd, Jeremy D. Semrau, William E. Antholine, J. I. Han, James A. Zahn, Jeffrey M. Boyd, Arlene M. de la Mora e Alan A. DiSpirito. "The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath". Journal of Bacteriology 185, n. 19 (1 ottobre 2003): 5755–64. http://dx.doi.org/10.1128/jb.185.19.5755-5764.2003.
Hedegård, Erik Donovan, e Ulf Ryde. "Molecular mechanism of lytic polysaccharide monooxygenases". Chemical Science 9, n. 15 (2018): 3866–80. http://dx.doi.org/10.1039/c8sc00426a.
Itoh, Shinobu, e Shunichi Fukuzumi. "Dioxygen Activation by Copper Complexes. Mechanistic Insights into Copper Monooxygenases and Copper Oxidases". Bulletin of the Chemical Society of Japan 75, n. 10 (ottobre 2002): 2081–95. http://dx.doi.org/10.1246/bcsj.75.2081.
Maiti, Debabrata, Amy A. Narducci Sarjeant e Kenneth D. Karlin. "Copper−Hydroperoxo-Mediated N-Debenzylation Chemistry Mimicking Aspects of Copper Monooxygenases". Inorganic Chemistry 47, n. 19 (6 ottobre 2008): 8736–47. http://dx.doi.org/10.1021/ic800617m.
Tesi sul tema "Copper monooxygenases":
Gómez-Piñeiro, Rogelio Javier. "Experimental and theoretical investigation of bioinspired mononuclear copper complexes". Electronic Thesis or Diss., Aix-Marseille, 2021. http://theses.univ-amu.fr.lama.univ-amu.fr/211213_GOMEZPINEIRO_886mtbc444s58hp471nxwde_TH.pdf.
Lytic polysaccharide monooxygenases (LPMO) break down polysaccharides and are greatly studied in the context of biomass conversion. They contain a mononuclear copper center which is studied by its magnetic properties. The mechanism of reaction and its intermediates are still unknown. We use a large set of well-known complexes to develop a protocol to predict the magnetic properties of copper systems using computational calculations. This protocol was applied to LPMO models and to an LPMO-inspired tripeptidic complex to elucidate their structural and spectroscopic properties. In addition, we produced a series of complexes to capture potential high-valent reaction intermediates of LPMO. Eventually, the reactivity of one specific complex was studied for its capacity to produce formate in alcohol solvents. Formate was produced at around 120% conversion. Future generations of ligands and complexes were also synthesized and envisioned to understand the reaction pathways of LPMO
Munzone, Alessia. "Structure-reactivity relationship of the copper-dependent lytic polysaccharide monooxygenase". Electronic Thesis or Diss., Aix-Marseille, 2021. http://theses.univ-amu.fr.lama.univ-amu.fr/210316_MUNZONE_559lhuy192l910eww669so_TH.pdf.
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes involved in the breakdown of recalcitrant polysaccharides, such as cellulose and chitin. The active site copper ion is coordinated by a very unusual coordination motif, consisting of two fully conserved histidines, one of which is located at the N-terminus and binds copper by both its the side chain nitrogen and the free amino terminal group. Such organization, known as “histidine brace” motif allows the oxidative cleavage of glycosidic bonds in recalcitrant polysaccharides, in the presence of dioxygen or hydrogen peroxide and an electron donor. The objectives of the present work have been pursued via an interdisciplinary approach, using tools and fundamental concepts that span from biology to chemistry. The focus was firstly addressed on the natural properties of the active site in the bacterial LPMOs belonging to the AA10 subfamily. Notably, the variability of a second coordination sphere alanine residue (~ 4 Å from the copper ion) was firstly investigated, leading to the discovery of new enzymes with unusual active-site features. The role of active site alanine was then probed by exploring the mutational effect induced by the other occurring residues on both the activity and the physico-chemical properties on the model enzyme SmAA10. Our results emphasize that this unusual coordination motif imparts unique structural and functional features to the copper centre. Furthermore, the SmAA10 active site variants allowed us to create original metal binding sites with the perspective of exploring new abiological metal-based biocatalytic reactions
Antypas, Elias J. "The characterization of Menkes copper transporter and dopamine ß- monooxygenase carboxy-terminus in neuroendocrine cells". Connect to full text in OhioLINK ETD Center, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1213789670.
"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences." Title from title page of PDF document. Bibliography: p. 126-146.
Antypas, Elias Joseph. "The Characterization of Menkes Copper Transporter and Dopamine ß-monooxygenase Carboxy-Terminus in Neuroendocrine Cells". University of Toledo Health Science Campus / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=mco1213789670.
Menil, Sidiky. "Cascade bi-enzymatique autosuffisante in vivo : le jeu des plasmides". Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0040.
Growing attention is paid to multienzymatic cascades to develop more efficient synthetic processes. However, in in cellulo process, the control of the simultaneous heterologous expression of several genes in the same host is often difficult and can lead to imbalances in the reaction flow. To exploit the benefits of cascades, activities of each step have to be adjusted and thus, cellular biocatalysts capable of programming enzymes stoichiometry have to be constructed. In this work, to modulate the stoichiometry of two enzymes in vivo, we developed an original approach based on the copy number per cell of plasmids (PCN) used as vectors. The PCN is regulated in bacteria by three main mechanisms leading, according to the replicon, to low, medium or high PCN. As proof of concept, we chose a self-sufficient system combining an Alcohol Dehydrogenase (ADH) and a Baeyer-Villiger MonoOxygenase (BVMO), both NADP(H)-dependent. Several recombinant plasmids harboring both genes were designed and combined in E. coli. Coexpression strains constructed were compared in terms of PCN, enzyme production and activity. We showed the importance of a judicious choice of plasmids combination and the existence of a correlation between enzymes ratios and activity. Our biocatalysts ranged from an inactive system to a system with a TTN of about 6000. This system allowed the synthesis of lactones of industrial interest, dihydrocoumarin and caprolactone, via double oxidation of indanol and cyclohexanol. Finally, based on this plasmids combination model, three new cellular biocatalysts combining ADH with various BVMOs were designed to broaden the range of esters and lactones synthesizable from alcohols
Menil, Sidiky. "Cascade bi-enzymatique autosuffisante in vivo : le jeu des plasmides". Electronic Thesis or Diss., Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0040.
Growing attention is paid to multienzymatic cascades to develop more efficient synthetic processes. However, in in cellulo process, the control of the simultaneous heterologous expression of several genes in the same host is often difficult and can lead to imbalances in the reaction flow. To exploit the benefits of cascades, activities of each step have to be adjusted and thus, cellular biocatalysts capable of programming enzymes stoichiometry have to be constructed. In this work, to modulate the stoichiometry of two enzymes in vivo, we developed an original approach based on the copy number per cell of plasmids (PCN) used as vectors. The PCN is regulated in bacteria by three main mechanisms leading, according to the replicon, to low, medium or high PCN. As proof of concept, we chose a self-sufficient system combining an Alcohol Dehydrogenase (ADH) and a Baeyer-Villiger MonoOxygenase (BVMO), both NADP(H)-dependent. Several recombinant plasmids harboring both genes were designed and combined in E. coli. Coexpression strains constructed were compared in terms of PCN, enzyme production and activity. We showed the importance of a judicious choice of plasmids combination and the existence of a correlation between enzymes ratios and activity. Our biocatalysts ranged from an inactive system to a system with a TTN of about 6000. This system allowed the synthesis of lactones of industrial interest, dihydrocoumarin and caprolactone, via double oxidation of indanol and cyclohexanol. Finally, based on this plasmids combination model, three new cellular biocatalysts combining ADH with various BVMOs were designed to broaden the range of esters and lactones synthesizable from alcohols
Shin, Jieun. "Investigating the Catalytic Mechanisms of Bio-degrading Copper Proteins: Multi-copper Oxidases (MCOs) and Lytic Polysaccharide Monooxygenases (LPMOs)". Thesis, 2021. https://thesis.library.caltech.edu/14252/5/Jieun-Shin_PhD-Thesis_May2021_Final.pdf.
Lignin and cellulose comprise a large portion of the renewable biomass on Earth. However, substantially due to laborious course of processing, the conversion efficiency of these biomaterials to accessible biofuel is very low. Therefore, effective depolymerization and utilization of these biopolymers are requirements for environmentally friendly and sustainable energy development. In the hope of finding solutions to these biomass utilization challenges, there have been growing interests in using biodegrading metalloenzymes as active biocatalysts. However, there still remain many questions regarding mechanistic details of enzyme catalysis and effective application of these enzymes. This thesis focuses on investigating the redox chemistry involved in the catalytic mechanisms of two main lignin- and cellulose- degrading copper enzymes: multicopper oxidases (MCOs) and lytic polysaccharide monooxygenases (LPMOs).
MCOs are capable of aerobic oxidation of lignin as their primary function, but the nature of their substrate variability also allows the oxidation of not only diverse high potential organic and inorganic complexes, but also earth abundant divalent metal ions such as manganese. LPMOs, on the other hand, enable the cleavage of glycosidic bonds in recalcitrant insoluble cellulosic substances, which are not degradable by other hydrolytic enzymes such as endoglucanases and cellulobiohydrolases.
It is remarkable that nature has created such versatile enzymes with specific active site metals and redox-active amino acids involved in electron transfer, which contribute to substrate oxidation as well as enzyme survival against oxidative damage during catalysis. By gaining a deeper understanding of how these enzymes work, we could greatly enhance current usage efficiencies and develop more energy-efficient biocatalysts.
Chapter I gives an introduction to biological coppers, two groups of bio-degrading copper enzymes: multicopper oxidases (MCOs) and lytic polysaccharide monooxygenases (LPMOs), and the role of redox-active amino acids in electron transfer and enzyme catalysis. For the MCO work, a thermophilic laccase (Tth-lac) from Thermus thermophilus HB27 and a CotA laccase (CotA-lac) from Bacillus Subtilis were studied. For the LPMO work, two cellulose active LPMOs (ScLPMO10B and ScLPMO10C) and a chitin active LPMO (BlLPMO10A) were studied.
Chapter II describes thermodynamic aspects of Tth-lac catalysis. The temperature dependence of the formal potential of type I copper (CuT1) in Tth-lac is reported, and the interplay between many competing dynamic and thermodynamic factors which results in thermostability and activity of Tth-lac is discussed.
Chapter III reports the electron transfer (ET) kinetics data obtained with Tth-lac using the transient absorption spectroscopy. The results of photochemical electron/hole transfer studies indicate that the chains of Trp and Tyr can participate in electron transfer through Tth-lac, which could potentially have a role in enzyme catalysis as well.
Chapter IV discusses the protective role of a Trp/Tyr pair positioned close to the trinuclear copper cluster (TNC) in Tth-lac. It is indeed remarkable that laccases are capable of utilizing the power of oxygen to catalyze the oxidation of diverse high-potential substrates. But, as a tradeoff, the utilization of dioxygen can make the enzyme highly susceptible to oxidative damage. Chapter IV provides supporting evidence that led us to conclude that the TNC-proximal Trp/Tyr pair functions as an internal antioxidant for prolonging the enzyme lifetime.
Chapter V describes investigations on the factors that affect MCO catalysis, which include the potentials of the active site coppers, possible reactive intermediates, and common structural motifs. Based on the structural homology between Tth-lac and CotA-lac, some preliminary work done on CotA-lac is also reported.
Chapter VI outlines the work on LPMOs. After the successful expression and purification of ScLPMO10B, ScLPMO10B and BlLPMO10A, standard activity assays were done with insoluble cellulose and chitin substrates to confirm the enzyme activity. The results are compared with that from the photo-degradation experiments to investigate if the photochemically generated Cu(III) species are active intermediates in LPMO catalysis.
Chapter VII reports the results on bioinformatics analysis on the distribution of vicinal amino acids in different enzyme classes. This study was to examine the biological significance of amino acid pairs and clusters existing in many different enzyme classes, with vicinal surface tyrosines in CotA-lac as an underlying motivation behind the work.
This thesis demonstrates that MCOs and LPMOs are truly versatile enzymes which can oxidize such diverse refractory substrates, and there could be multiple pathways that the enzymes achieve this task. As shown so far, not only the active site metals but also the chain of redox-active amino acids as well as metal coordinating residues can contribute to enzyme catalysis.
蘇柏瑋. "Models of the Particulate Methane Monooxygenase(pMMO): Trinuclear Copper Clusters". Thesis, 2011. http://ndltd.ncl.edu.tw/handle/12381536418153308701.
國立臺灣師範大學
化學系
100
In this study, two new ligands 7-Impy and 7-MeImpy have been synthesized, and they can coordinate with 3 equivalents of CuI ions to form a trinuclear copper complex [CuICuICuI(7-Impy)](BF4) and [CuICuICuI(7-MeImpy)](BF4). These ligands are similar to our previous developed 7-Dipy ligand in the scaffold to trap three CuI ions. It is known that the hydroxylation of alkane molecules catalyzed by trinuclear copper complexes through the “oxene” insertion mechanism. The active “oxene” with a “1D” spin state will have lower reaction energy barrier when it is tuned by three copper ions. In this study, these new catalysts, [CuICuICuI(7-ImPy)](BF4) and [CuICuICuI(7-MeImPy)](BF4), are also able to catalyze the oxidation of cyclohexane converting to cyclohexanol and cyclohexanone. Compared to our previous developed 7-Dipy ligand, the catalytic reaction is more favorable for the product of cyclohexanol. In this study, we replaced traditional heating by microwave for the ligand synthesis. Microwave can enhance internal heating efficiently, which significantly reduce the reaction time, increase the purity, and reduce the byproducts. In addition, for proving the reaction catalyzed by our trinuclear copper cluster via the O-atom insertion mechanism or radical mechanism, we designed a series of experiments using 5,5-Dimethyl-Pyrroline-N-Oxide (DMPO), which is very sensitive to radical. We added DMPO in catalytic reaction, and measured EPR while in the reaction. We found that there are no radical EPR peaks related to DMPO derivatives, similar to the case of 7-Dipy.
Chen, Chang-Li, e 陳昌立. "Copper Ions and The Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath)". Thesis, 2004. http://ndltd.ncl.edu.tw/handle/bk48ja.
國立清華大學
化學系
92
Copper ions play an essential role in particulate methane monooxygenase (pMMO) from Methylococcus capsulatus (Bath). The particulate methane monooxygenase (pMMO) contains 15 reduced copper ions which are arranged in five trinuclear clusters. Two of these clusters were subsequently found to participate in dioxygen chemistry and hydrocarbon hydroxylation chemistry, called C-clusters. The remaining copper ions were in the reduced d10 state, and were thought to be responsible for channeling electrons to the C-clusters from NADH, called E-clusters. The low temperature EPR spectrum of as-isolated pMMO was deconvoluted into a type 2 Cu(II) signal and a broad, but nearly isotropic EPR signal centered at g ~ 2.1. Earlier magnetization and magnetic susceptibility measurements have suggested that the latter EPR signal, which is not sensitive to microwave power saturation, arise from a ferromagnetically exchange-coupled trinuclear Cu(II) cluster with J = 15�{20 cm–1 and with a zero-field splitting D of +0.018cm-1 (175 G) and E value of 0.005 cm-1 (50 G). By combining EPR spectroscopy and rapid cryogenically trap, we successfully observed the different oxidative phases of the turnover cycle and practically proved the catalytic mechanisms of pMMO. Processing cell growth in a fermentor adapted with a hollow-fiber bioreactor, we successfully prepared the (Cu, Zn)-pMMO. The bulk of the copper ions of the E-clusters have been replaced by divalent Zn ions in (Cu, Zn)-pMMO. The Cu and Zn contents in the (Zn, Cu)-pMMO were determined by both ICP-MS and x-ray absorption K-edge spectroscopy. Further characterization of the (Zn, Cu)-pMMO was provided by low temperature electron paramagnetic spectroscopy during reductive titration and hydrocarbon hydroxylation. These studies indicate that the (Zn, Cu)-pMMO is still capable of supporting the activation of dioxygen, but that the replacement of the E-cluster copper ions has compromised the ability of the protein to mediate the transfer of reducing equivalents to the C-clusters. These observations provide strong support for the electron transfer and catalytic roles that we have previously proposed for the E-cluster and C-cluster copper ions, respectively.
Yang, Bing-Gong, e 楊秉恭. "Models for the Trinuclear Copper Clusters of the Particulate Methane Monooxygenase from Methanotrophic Bacteria: Synthesis, Spectroscopic Characterization of Trinuclear Copper Complexes". Thesis, 2006. http://ndltd.ncl.edu.tw/handle/04856074935855023692.
國立中央大學
化學研究所
94
Recent DFT electronic calculations of a trinuclear copper cluster bis(��3-oxo)trinuclear copper(II, II, III) complex have showed that this structure harnesses a singlet “oxene”, mimicking one of the C-clusters in the particulate methane monooxygenase (pMMO), an important membrane enzyme that mediate the facile hydroxylation of methane and other small hydrocarbons. A series of supporting ligands that are capable to trap three copper ions toward developing a model compound to mimic this chemistry, we have designed and synthesized. Oxygenation of their corresponding [Cu3(I, I, I)L](X) complexes of these ligands leads to the formation of [Cu3(II, II, II)L(O)](X)2 (L = 7-Et, 7-Me, 6-Et, 6-Me; X = ClO4- and BF4-) through mass spectrometry analysis. Only one oxygen atom is locked in the trinuclear copper(II, II, II) complex. When the [Cu3(II, II, II)L(O)](X)2 complex is treated with three equivalent amounts of benzoin and triethylamine in CH3CN, and the solution purged by dioxygen, the benzoin is oxidized to benzil, which in turn is cleaved by further oxidation and hydrolyzes to 2 benzoic acid molecules. This chemistry is mediated by efficient oxo-transfer from the bis(μ3-oxo)trinuclear copper(II, II, III) complex to the benzil, as verified by 18O2 isotope labeling experiments and subsequent GC-MS analysis. We propose a mechanism involving intermolecular oxo-insertion across the C-C bond of the benzil by the bis(μ3-oxo)Cu(II)Cu(II)Cu(III) trinuclear copper intermediate.
Capitoli di libri sul tema "Copper monooxygenases":
Réglier, Marius, e Catherine Belle. "Copper, Mononuclear Monooxygenases". In Encyclopedia of Metalloproteins, 723–29. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_97.
Tyeklár, Zoltán, e Kenneth D. Karlin. "Functional Models for Hemocyanin and Copper Monooxygenases". In Bioinorganic Chemistry of Copper, 277–91. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-6875-5_22.
Blackburn, Ninian J. "Chemical and Spectroscopic Studies on Dopamine-β-Hydroxylase and other Copper Monooxygenases". In Bioinorganic Chemistry of Copper, 164–83. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-6875-5_14.
Osborne, Robert L., e Judith P. Klinman. "Insights into the Proposed Copper-Oxygen Intermediates that Regulate the Mechanism of Reactions Catalyzed by Dopamine β-Monooxygenase, Peptidylglycine α-Hydroxylating Monooxygenase, and Tyramine β-Monooxygenase". In Copper-Oxygen Chemistry, 1–22. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118094365.ch1.
Chan, Sunney I., Hiep-Hoa T. Nguyen, Andrew K. Shiemke e Mary E. Lidstrom. "The Copper Ions in the Membrane-Associated Methane Monooxygenase". In Bioinorganic Chemistry of Copper, 184–95. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-6875-5_15.
Klinman, Judith P., Joseph A. Berry e Gaochao Tian. "New Probes of Oxygen Binding and Activation: Application to Dopamine β-Monooxygenase". In Bioinorganic Chemistry of Copper, 151–63. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-6875-5_13.
Sazinsky, Matthew H., e Stephen J. Lippard. "Methane Monooxygenase: Functionalizing Methane at Iron and Copper". In Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases, 205–56. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-12415-5_6.
Castillo, Ivan. "Inorganic Models of Lytic Polysaccharide Monooxygenases". In Copper Bioinorganic Chemistry, 187–209. WORLD SCIENTIFIC, 2023. http://dx.doi.org/10.1142/9789811269493_0006.
Bhatia, B., T. Punniyamurthy e J. Iqbal. "Oxidation of the C—H bond". In Asymmetric Oxidation Reactions, 5–18. Oxford University PressOxford, 2001. http://dx.doi.org/10.1093/oso/9780198502012.003.0002.
"Copper-Containing Monooxygenase". In Encyclopedia of Metalloproteins, 735. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_100378.
Rapporti di organizzazioni sul tema "Copper monooxygenases":
Xu, Jin-Rong, e Amir Sharon. Comparative studies of fungal pathogeneses in two hemibiotrophs: Magnaporthe grisea and Colletotrichum gloeosporioides. United States Department of Agriculture, maggio 2008. http://dx.doi.org/10.32747/2008.7695585.bard.