Relevant bibliographies by topics / Cu cofactor

Academic literature on the topic 'Cu cofactor'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Cu cofactor"

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Murakawa, Takeshi, Kazuo Kurihara, Mitsuo Shoji, Chie Shibazaki, Tomoko Sunami, Taro Tamada, Naomine Yano, et al. "Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing." Proceedings of the National Academy of Sciences 117, no. 20 (May 5, 2020): 10818–24. http://dx.doi.org/10.1073/pnas.1922538117.

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Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions.
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Kwok, Man Long, Xue Lei Hu, Qi Meng, and King Ming Chan. "Whole-transcriptome sequencing (RNA-seq) analyses of the zebrafish liver cell line, ZFL, after acute exposure to Cu2+ ions." Metallomics 12, no. 5 (2020): 732–51. http://dx.doi.org/10.1039/d0mt00005a.

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Goto, Norika, Hirokazu Hara, Mao Kondo, Naomi Yasuda, Tetsuro Kamiya, Kensuke Okuda, and Tetsuo Adachi. "Hydrogen sulfide increases copper-dependent neurotoxicity via intracellular copper accumulation." Metallomics 12, no. 6 (2020): 868–75. http://dx.doi.org/10.1039/d0mt00015a.

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Morpurgo, L., E. Agostinelli, O. Befani, and B. Mondovì. "Reactions of bovine serum amine oxidase with NN-diethyldithiocarbamate. Selective removal of one copper ion." Biochemical Journal 248, no. 3 (December 15, 1987): 865–70. http://dx.doi.org/10.1042/bj2480865.

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NN-Diethyldithiocarbamate (DDC) was able to bind, at 1.0 mM concentration, only about 50% the Cu(II) ions of bovine plasma amine oxidase. Under reducing conditions, this Cu(II) was removed with inactivation of the enzyme. Up to 90% activity could be recovered by treatment with excess Cu(II). The organic cofactor, sensitive to carbonyl reagents, was reduced in the half-Cu-depleted protein and no longer bound phenylhydrazine. The fully reacted protein, in the presence of 10 mM-DDC, lost 50% Cu(II) upon storage at -20 degrees C, but in this case the residual Cu(II) was in the DDC-bound form and the cofactor was in the oxidized state, as it could still bind phenylhydrazine. In the presence of DDC, the rate of reaction with phenylhydrazine was always low, even at 50% DDC saturation, and all derivatives showed identical modifications of the optical and e.p.r. spectra with respect to the phenylhydrazone of the native protein. It is concluded that the two Cu(II) ions are not equivalent, that removal of a single Cu(II) is sufficient to inhibit the re-oxidation of the organic cofactor, and that both Cu(II) ions are in some way involved in the reaction with phenylhydrazine. After reaction with DDC, the optical and e.p.r. spectra of 63Cu(II)-amine oxidase and of 63Cu(II)-carbonic anhydrase [Morpurgo, Desideri, Rigo, Viglino & Rotilio (1983) Biochim. Biophys. Acta 746, 168-175] are very similar and show distorted equatorial co-ordination to Cu(II) of two sulphur atoms and two magnetically equivalent nitrogen atoms.
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Kwok, Man Long, and King Ming Chan. "Functional characterization of copper transporters zCtr1, zAtox1, zAtp7a and zAtp7b in zebrafish liver cell line ZFL." Metallomics 11, no. 9 (2019): 1532–46. http://dx.doi.org/10.1039/c9mt00159j.

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Tasaki, Eisuke, Kazuya Kobayashi, Kenji Matsuura, and Yoshihito Iuchi. "Long-Lived Termite Queens Exhibit High Cu/Zn-Superoxide Dismutase Activity." Oxidative Medicine and Cellular Longevity 2018 (2018): 1–8. http://dx.doi.org/10.1155/2018/5127251.

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In most organisms, superoxide dismutases (SODs) are among the most effective antioxidant enzymes that regulate the reactive oxygen species (ROS) generated by oxidative energy metabolism. ROS are considered main proximate causes of aging. However, it remains unclear if SOD activities are associated with organismal longevity. The queens of eusocial insects, such as termites, ants, and honeybees, exhibit extraordinary longevity in comparison with the nonreproductive castes, such as workers. Therefore, the queens are promising candidates to study the underlying mechanisms of aging. Here, we found that queens have higher Cu/Zn-SOD activity than nonreproductive individuals of the termite Reticulitermes speratus. We identified three Cu/Zn-SOD sequences and one Mn-SOD sequence by RNA sequencing in R. speratus. Although the queens showed higher Cu/Zn-SOD activity than the nonreproductive individuals, there were no differences in their expression levels of the Cu/Zn-SOD genes RsSOD1 and RsSOD3A. Copper (Cu2+ and Cu+) is an essential cofactor for Cu/Zn-SOD enzyme activity, and the queens had higher concentrations of copper than the workers. These results suggest that the high Cu/Zn-SOD activity of termite queens is related to their high levels of the cofactor rather than gene expression. This study highlights that Cu/Zn-SOD activity contributes to extraordinary longevity in termites.
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Song, Haiyan, Chunling Ma, Pi Liu, Chun You, Jianping Lin, and Zhiguang Zhu. "A hybrid CO2 electroreduction system mediated by enzyme-cofactor conjugates coupled with Cu nanoparticle-catalyzed cofactor regeneration." Journal of CO2 Utilization 34 (December 2019): 568–75. http://dx.doi.org/10.1016/j.jcou.2019.08.007.

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Whittaker, Mei M., and James W. Whittaker. "Cu(I)-dependent Biogenesis of the Galactose Oxidase Redox Cofactor." Journal of Biological Chemistry 278, no. 24 (April 1, 2003): 22090–101. http://dx.doi.org/10.1074/jbc.m300112200.

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Young, Tessa R., and Zhiguang Xiao. "Principles and practice of determining metal–protein affinities." Biochemical Journal 478, no. 5 (March 10, 2021): 1085–116. http://dx.doi.org/10.1042/bcj20200838.

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Metal ions play many critical roles in biology, as structural and catalytic cofactors, and as cell regulatory and signalling elements. The metal–protein affinity, expressed conveniently by the metal dissociation constant, KD, describes the thermodynamic strength of a metal–protein interaction and is a key parameter that can be used, for example, to understand how proteins may acquire metals in a cell and to identify dynamic elements (e.g. cofactor binding, changing metal availabilities) which regulate protein metalation in vivo. Here, we outline the fundamental principles and practical considerations that are key to the reliable quantification of metal–protein affinities. We review a selection of spectroscopic probes which can be used to determine protein affinities for essential biological transition metals (including Mn(II), Fe(II), Co(II), Ni(II), Cu(I), Cu(II) and Zn(II)) and, using selected examples, demonstrate how rational probe selection combined with prudent experimental design can be applied to determine accurate KD values.
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Chen, Guang, Jia Li, Huimin Han, Ruiying Du, and Xu Wang. "Physiological and Molecular Mechanisms of Plant Responses to Copper Stress." International Journal of Molecular Sciences 23, no. 21 (October 26, 2022): 12950. http://dx.doi.org/10.3390/ijms232112950.

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Copper (Cu) is an essential micronutrient for humans, animals, and plants, and it participates in various morphological, physiological, and biochemical processes. Cu is a cofactor for a variety of enzymes, and it plays an important role in photosynthesis, respiration, the antioxidant system, and signal transduction. Many studies have demonstrated the adverse effects of excess Cu on crop germination, growth, photosynthesis, and antioxidant activity. This review summarizes the biological functions of Cu, the toxicity of excess Cu to plant growth and development, the roles of Cu transport proteins and chaperone proteins, and the transport process of Cu in plants, as well as the mechanisms of detoxification and tolerance of Cu in plants. Future research directions are proposed, which provide guidelines for related research.
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Dissertations / Theses on the topic "Cu cofactor"

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Sansone, Assunta. "The role of [CU-ZN]-cofactored superoxide dismutase in salmonella virulence." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246768.

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Book chapters on the topic "Cu cofactor"

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Maurya, Radheshyam, and Madhulika Namdeo. "Superoxide Dismutase: A Key Enzyme for the Survival of Intracellular Pathogens in Host." In Reactive Oxygen Species [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.100322.

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Superoxide dismutase (SOD) is a crucial enzyme required to maintain the redox potential of the cells. It plays a vital role in protecting normal cells from reactive oxygen species (ROS) produced during many intracellular pathogens infections. SOD removes excess superoxide radicals (O2−) by converting them to hydrogen peroxide (H2O2) and molecular oxygen (O2). Several superoxide dismutase enzymes have been identified based on the metal ion as a cofactor. Human SOD differs from the intracellular pathogens in having Cu/Zn and Mn as metal cofactors. However, SOD of intracellular pathogens such as Trypanosoma, Leishmania, Plasmodium, and Mycobacterium have iron (Fe) as metal cofactors. Iron Superoxide Dismutase (FeSOD) is an essential enzyme in these pathogens that neutralizes the free radical of oxygen (O−) and prevents the formation of Peroxynitrite anion (ONOO−), helping the pathogens escape from redox-based cytotoxic killing. Moreover, most intracellular bacteria hold MnSOD or FeSOD in their cytoplasm such as Salmonella and Staphylococcus, whereas periplasm of some pathogenic bacteria and fungi are also cofactors with Cu/Zn and identified as CuZnSOD. This chapter will review the various types SOD present in intracellular pathogens and their role in the survival of these pathogens inside their host niche.
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SHANBHAG, V. M., and ARTHUR E. MARTELL. "Oxidative Deamination of Amino Acids by Molecular Oxygen with Pyridoxal Phosphate and Cu(II) Ion as Catalysts." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors, 365–69. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50078-9.

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