Copper biochemical activity

Benzo-l,3-oxathiole derivatives have been reported with remarkable pharmaceutical and biochemical activities. In 2008, Bao and co-workers described a novel and efficient copper(i)-catalyzed one-pot cascade process for the formation of 2-iminobenzo-l,3-oxathioles from readily available... 

Kensler, T.W. and Trush, M.A, (1983). Inhibition of oxygen radical metabolism in phorbol ester-activated polymorphonuclear leukocytes by an antitumor promoting copper complex with superoxide dismutase-mimetic activity. Biochem. Pharmacol. 32, 3485-3487. 

Copper is an essential micronutrient required in the growth of both plants and animals. In humans, it helps in the production of blood haemoglobin. In plants, copper is an important component of proteins found in the enzymes that regulate the rate of many biochemical reactions in plants. Plants would not grow without the presence of these specific enzymes. Research projects show that copper promotes seed production and formation, plays an essential role in chlorophyll formation and is essential for proper enzyme activity, disease resistance and regulation of water in plants (Rehm and Schmitt, 2002). 

Moffitt, A.E., Jr. and S.D. Murphy. 1973. Effect of excess and deficient copper intake on rat liver microsomal enzyme activity. Biochem. Pharmacol. 22 1463-1476. 

Moreau, J.-F. and Hancock, R. G. V. (1996). Chrono-cultural technique based on the instrumental neutron activation analysis of copper-based artifacts from the contact period of northeastern North America. In Archaeological Chemistry organic, inorganic and biochemical analysis, ed. Orna, M. V., ACS Symposium Series 625, Washington, DC, American Chemical Society, pp. 64-82. 

There has been enormous activity in the field of copper(I)-dioxygen chemistry in the last 25 years, with our information coming from both biochemical-biophysical studies and to a very important extent from coordination chemistry. This has resulted in the structural and spectroscopic characterization of a large number of copper dioxygen complexes, some of which are represented in Figure 14.2. The complex F, first characterized in a synthetic system was subsequently established to be present in oxy-haemocyanin, and is found in derivatives of tyrosinase and catechol oxidase, implying its involvement in aromatic hydroxylations in both enzymes and chemical systems. 

An excess of zinc will cause problems in humans. Excessive doses can lead to biochemical control system damage, while doses slightly higher than optimal can cause disorders in iron and copper metabolism, resulting in incurable anemia, decrease in activity of zinc protein enzymes, and pancreas and kidney damage (Boularbah et ah, 1999 Seiler et ah, 1994). Increased levels of zinc have been observed in nuclei of neoplastic cells and in cases of acute dental caries, however its role in these diseases has not been explained. 

Probing Metalloproteins Electronic absorption spectroscopy of copper proteins, 226, 1 electronic absorption spectroscopy of nonheme iron proteins, 226, 33 cobalt as probe and label of proteins, 226, 52 biochemical and spectroscopic probes of mercury(ii) coordination environments in proteins, 226, 71 low-temperature optical spectroscopy metalloprotein structure and dynamics, 226, 97 nanosecond transient absorption spectroscopy, 226, 119 nanosecond time-resolved absorption and polarization dichroism spectroscopies, 226, 147 real-time spectroscopic techniques for probing conformational dynamics of heme proteins, 226, 177 variable-temperature magnetic circular dichroism, 226, 199 linear dichroism, 226, 232 infrared spectroscopy, 226, 259 Fourier transform infrared spectroscopy, 226, 289 infrared circular dichroism, 226, 306 Raman and resonance Raman spectroscopy, 226, 319 protein structure from ultraviolet resonance Raman spectroscopy, 226, 374 single-crystal micro-Raman spectroscopy, 226, 397 nanosecond time-resolved resonance Raman spectroscopy, 226, 409 techniques for obtaining resonance Raman spectra of metalloproteins, 226, 431 Raman optical activity, 226, 470 surface-enhanced resonance Raman scattering, 226, 482 luminescence... 

The biochemical importance of flavin coenzymes ap-pears to be their versatility in mediating a variety of redox processes, including electron transfer and the activation of molecular oxygen for oxygenation reactions. An especially important manifestation of their redox versatility is their ability to serve as the switch point from the two-electron processes, which predominate in cytosolic carbon metabo-lism, to the one-electron transfer processes, which predomi-nate in membrane-associated terminal electron-transfer pathways. In mammalian cells, for example, the end products of the aerobic metabolism of glucose are C02 and NADH (see chapter 13). The terminal electron-transfer pathway is a membrane-bound system of cytochromes, nonheme iron proteins, and copper-heme proteins—all one-electron acceptors that transfer electrons ultimately to 02 to produce H20 and NAD+ with the concomitant production of ATP from ADP and P . The interaction of NADH with this pathway is mediated by NADH dehydrogenase, a flavoprotein that couples the two-electron oxidation of NADH with the one-electron reductive processes of the membrane. 

Ortmans I, Moucheron C, Kirsch-De Mesmaeker A (1998) Ru(ll) polypyridine complexes with a high oxidation power. Comparison between their photoelectrochemisty with transparent SnC>2 and their photochemistry with desoxyribonucleic acids. Coord Chem Rev 168 233-271 Ozawa T, Ueda J, Flanaki A (1993) Copper(ll)-albumin complex can activate hydrogen peroxide in the presence of biological reductants first ESR evidence for the formation of hydroxyl radical. Biochem Mol Biol Int 29 247-253... 

Reddy PAN, Santra BK, Nethaji M, Chakravarty AR. Metal-assisted hght induced DNA cleavage activity of 2-metrhylthiophenylsalicyamide Schiff base copper(II) complexes having planar heterocylic bases. / Inorg Biochem 2004 98 377-86. 

Saxena, A. K., Saxena, P., Wu, X., Obrenovich, M., Weiss, M. F., and Monnier, V. M., Protein aging by carboxymethylation of lysines generates sites for divalent metal and redox active copper binding Relevance to diseases of glycoxidative stress. Biochem. Biophys. Res. Commun. 260,332-338 (1999). 

Relevant to the conflicting reports of copper versns nickel reqnirements for enzyme activity,biochemical stndies demonstrated the existence of a labile nickel associated with the a snbnnit of ACS/CODH. Very recently, model stndies on a metal-ion captnre of a peptide-backbone, nonlabile [MN2S2] (26) nnit have established the capability of snch a nickel dithiolate to bind exogeneons metals. A qualitative ranking of the binding ability of complex (26) with Zn +, Cn+, and Ni + was established by a metal-ion displacement experiment (Zn + < < Cn+), as shown in Scheme 9. ... 

The mechanisms of catalysis and copper-dependent trafficking of the Menkes protein have been summarized in a recent review. Biochemical studies indicated that mutation of six metal-binding sites did not abolish the catalytic activity of Menkes ATPase and hence it was considered that these motifs were not essential for copper translocation. However, the binding of copper to these sites increased the affinity of the protein for copper translocation, which would involve the interaction between the binding sites and the cytosohc ATP-binding domain of ATP7A. Much further work is necessary to delineate the mechanism of this process. 

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