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Copper
Published in Brian D. Fath, Sven E. Jørgensen, Megan Cole, Managing Global Resources and Universal Processes, 2020
R. Parker David, F. Pedler Judith
Copper is an essential element for plant growth and is a component of many enzymes, including plastocyanin, and thus is an indispensable prosthetic group in Photosystem 2. Cu-containing proteins are also important in respiration (cytochrome c oxidase is the terminal oxidase of the mitochondrial electron chain), in detoxification of superoxide radicals (superoxide dismutase), and in lignification (polyphenol oxidase). Ascorbate oxidase, which contains eight Cu2+ ions, has been proposed as an indicator of plant Cu status, although its relevant biological function has yet to be determined.[10]
Medium Design for Cell Culture Processing
Published in Wei-Shou Hu, Cell Culture Bioprocess Engineering, 2020
In comparison, the copper ion, which has an even higher oxidative potential than Fe3+, is present only in small numbers of cellular proteins, many of which are extracellular or are involved in prevention of copper toxicity.5 Copper is provided at low levels in most traditional media, about three orders of magnitude lower than iron. Nevertheless, it plays a critical role as the cofactor in cytochrome C oxidase that catalyzes the last step of the electron transfer chain by reducing oxygen to water and pumping four protons across the mitochondrial inner membrane. Increasing copper levels in traditional media has been shown to facilitate the transition of glucose metabolism from a high flux state to low flux state in the late exponential growth phase. Since copper is highly oxidative, caution should be taken when raising copper to very high levels.
Biomarkers of selenium and copper status in patients with traumatic spinal cord injury
Published in Gary Bañuelos, Zhi-Qing Lin, Dongli Liang, Xue-bin Yin, Selenium Research for Environment and Human Health: Perspectives, Technologies and Advancements, 2019
J. Seelig, R.A. Heller, J. Hackler, L. Schomburg, A. Moghaddam, B. Biglari
Traumatic Spinal Cord Injury (TSCI) is damage of the spinal cord resulting in devastating loss of motor and sensory functions. This injury involves complex pathological mechanisms with massive oxidative stress and extensive inflammatory processes, which can bear the risk for permanent paraplegia (Alizadeh et al. 2019). Selenium (Se) is an essential factor for neuronal development, protects from neuron degeneration, and plays a key role in the antioxidative defense. Selenoprotein P (SELENOP) is the transport protein of Se and an essential survival factor for neurons (Pitts et al. 2014). Copper (Cu) serves as an important catalytic cofactor in redox chemistry, e.g., in superoxide dismutase or cytochrome C oxidase. Other copper-containing proteins are relevant for fundamental biological functions, such as lysyl oxidase for the maturation of the extracellular matrix or ceruloplasmin (CP) for the transport of Cu throughout the system. CP accounts for 95% of the Cu content in serum and protects tissue from iron-mediated oxidative damage (Guengerich 2018). Notably, serum Se via SELENOP and Cu via CP are inversely regulated in infection and acute phase response. As TSCI is associated with severe inflammation, we decided to study the potential alterations of the Se and Cu status as potential diagnostic and predictive parameters, as there is a clinical need for informative biomarkers particularly during the first 24 h after injury.
Development of new amphiphilic bio-organic assemblies for potential applications in iron-binding and targeting tumor cells
Published in Soft Materials, 2019
Mindy M. Hugo, Ipsita A. Banerjee
Cytochrome c oxidase is a vital enzyme in the electron transport chain and changes in its activity have been associated with increased production of mitochondrial ROS(89). To assess if the nanoassemblies had an effect on mitochondrial ROS production related to iron overload in HeLa cells, we examined the cytochrome c activity of the cells. Decrease in the absorbance of ferrocytochrome c due to its oxidation to ferricytochrome c by the enzyme cytochrome c oxidase was measured colorimetrically. Results obtained are shown in Table 1. Except in the case of Fmoc-ED-Tf, which showed very little change in activity over time, there was a decrease in activity of cytochrome c oxidase activity after 18 h in all cases. In previous studies it has been reported that decrease in cytochrome c activity may be caused by high mitochondrial ROS production, which consequently leads to less ATP production and ultimately damages cells (90). In general, higher cytochrome c activity was observed in the presence of the nanoassemblies compared to control cells, implying that mitochondrial ROS production may be mitigated by the nanoassemblies. The effects are more prominent in Fac treated cells. These results imply that the nanoassemblies may mitigate mitochondrial damage by chelating intracellular iron.
Biochemical and transcriptional analyses of cadmium-induced mitochondrial dysfunction and oxidative stress in human osteoblasts
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Cristina Monteiro, José Miguel P. Ferreira de Oliveira, Francisco Pinho, Verónica Bastos, Helena Oliveira, Francisco Peixoto, Conceição Santos
Complex IV (cytochrome c oxidase) specific activity was determined by measuring the oxidation of reduced cytochrome c at 550 nm (ε = 21.84 mM−1cm−1) in the presence or absence of 2.75-mM KCN. The assay was performed at 30 ºC in 50-mM K2HPO4 (pH 7.4), containing 0.2-µM rotenone, 0.2-µM antimycin. After 2 min the reaction was initiated by adding 11 µM reduced cytochrome c and enzyme activity measured for 3 min. Specific activity was calculated based on the molar absorptivity coefficient of cytochrome c (18.5 mM−1 cm−1)
Interactions of α -Lactalbumin and Cytochrome c with Langmuir Monolayers of Glycerophospholipids
Published in Journal of Dispersion Science and Technology, 2011
Wilhelm R. Glomm, Sondre Volden, Marit-Helen Glomm Ese, Øyvind Halskau
Bovine α-lactalbumin (α-La) is a 14.2 kDa globular calcium-binding milk protein which is a component of the lactose synthase complex. α-La binds to galactosyltransferase, promoting glucose binding and facilitating the synthesis of lactose in lactating mammary glands.[18] Previous in vitro studies have shown that α-La adopts a molten globular-like conformation when it interacts with membranes.[1-5] Cytochrome c (Cyt c) shuttles electrons between the two membrane-associated protein complexes cytochrome c reductase and cytochrome c oxidase on the inside of the inner mitochondrial membrane, and is a part of the mitochondrial production of ATP. It has been established using fluorescence measurements of monolayers[19] and solid-state 31P NMR[20] that Cyt c binds specifically to anionic phospholipids. Moreover, Cyt c has been demonstrated to form stable molten globules both at electrodes set up to mimic the in vivo redox reaction,[21] in association with anionic membranes, and in bulk solution.[12,22-25] Thus, the two proteins are both globular and mostly helical, amphitropic proteins of similar size and share the trait of being able to partially unfold as they interact with membranes and surfaces. Their charge properties are different, however, with α-La being an acidic while Cyt c being a basic protein. Herein, we address whether proteins and their trapped folding states can intercalate into already formed phospholipid monolayers, as well as the importance of global protein charge for interaction.