Biochemistry copper

In copper-containing proteins, three types of copper, classified on the basis of their visible, UV and EPR spectra, as originally proposed by one of the pioneers of copper biochemistry, Bo Malmstrom, are found. Types 1 and 2 have one copper atom, which has an intense blue colour in Type 1 and is almost colourless in Type 2 whereas Type 3 has an EPR-silent dicopper centre. More details of the three types are as follows ... 

Transition metal hydroperoxo species are well established as important intermediates in the oxidation of hydrocarbons (8,70,71). As they relate to the active oxygenating reagent in cytochrome P-450 monooxygenase, (porphyrin)M-OOR complexes have come under recent scmtiny because of their importance in the process of (poiphyrin)M=0 formation via 0-0 cleavage processes (72-74). In copper biochemistry, a hydroperoxo copper species has been hypothesized as an important intermediate in the catalytic reaction of the copper monooxygenase, dopamine P-hydroxylase (75,76). A Cu-OOH moiety has also been proposed to be involved in the disproportionation of superoxide mediated by the copper-zinc superoxide dismutase (77-78). Thus, model Cun-OOR complexes may be of... 

Linder MC, Hazegh-Axam M. Copper biochemistry and molecular biology. Am J CUn Nutr 1996 63 797S-811S. 

Pituitary Growth Factor (from human pituitary giand) [336096-71-0]. Purified by heparin and copper affinity chromatography, followed by chromatography on carboxymethyl cellulose (Whatman 52). [Rowe et al. Biochemistry 25 6421 1986.]... 

Nackerdien, Z., Rao, G., Cacciuttolo, M.A., Gajewski, E. and Dizdaroglu, M. (1991). Chemical nature of DNA-protein cross-links produced in mammalian chromatin by hydrogen peroxide in the presence of iron or copper ions. Biochemistry 30, 4872-4879. 

Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, Mougin C. 2002. Crystal structure of a four-copper laccase complexed with an arylamine Insights into substrate recognition and correlation with kinetics. Biochemistry 41 7325-7333. 

Tu, A.T., Friedrich CG Interaction of copper ion with guanosine and related compounds, Biochemistry, 7,4367,1968. 

Oxygen activation is a central theme in biochemistry and is performed by a wide range of different iron and copper enzymes. In addition to our studies of the dinuclear non-heme iron enzymes MMO and RNR, we also studied oxygen activation in the mononuclear non-heme iron enzyme isopenicillin N synthase (IPNS). This enzyme uses O2 to transform its substrate ACV to the penicillin precursor isopenicillin N [53], a key step in the synthesis of the important P-lactam antibiotics penicillins and cephalosporins [54, 55],... 

Rao, S. B. K., A. M. Tyryshkin et al. (2000). Inhibitory copper binding site on the spinach cytochrome bf complex Implications for Q0 site catalysis. Biochemistry 39 3285-3296. 

Smith, C.A., Anderson, B.F., Baker, H.M., and Baker, E.N. 1992. Metal substitution in transferrins the crystal structure of human copper-lactoferrin at 2.1-A resolution. Biochemistry 31 4527 -533. 

Lauren, DJ. and D.G. McDonald. 1987b. Acclimation to copper by rainbow trout, Salmo gairdneri biochemistry. Canad. Jour. Fish. Aquat. Sci. 44 105-111. 

Figure 5.1 Type I, II, and III copper center geometries. Dotted lines indicate possible ligands. (Adapted from Figure 5.4 of Cowan, J. A. Inorganic Biochemistry, An Introduction, 2nd ed Wiley-VCH, New York, 1997. Copyright 1997, Wiley-VCH.)...

Fig. 8. Model for the high affinity complex between horse Cc and CcO determined by Roberts and Pique (34). The backbone of horse Cc and CcO subunit II are shown with the side chains of selected lysines and acidic residues colored blue and red, respectively. The residue numbers on subunit II are for R. sphaeroides CcO. Van der Waals surfaces are shown for Cc heme and subunit II Trp143 and Met263. The CuA coppers are represented by green Corey-Pauling-Koltun models. Reprinted with permission from Ref. (18). Copyright 1999, American Society of Biochemistry and Molecular Biology.

Trombley, P. Q., Homing, N. S., Blackmore, L. J. (2000). Interactions between carnosine and zinc and copper implications for neuromodulation and neuroprotection. Biochemistry (Mosc) Jul 65 807-16. 

One of the intriguing questions in the biochemistry of copper is how it can function in rapid electron-transfer reactions2 when Cu(I) and Cu(II) have such drastically different preferences in coordination geometry. As we have already pointed above, four-coordinate Cu(II) complexes are square-planar, while the corresponding Cu(I) complexes tend to be... 

M. T. Graziani, A. L. Agro, G. Rotilio, D. Barra, and B. Mondovi, Parsley plastocyanin. The possible presence of sulfhydryl and tyrosine in the copper environment, Biochemistry 13, 804-809 (1974). 

Hamilton, G. A., In "Metal Ions in Biology Copper Proteins" Spiro, T. G., Ed. John Wiley and Sons New York, 1981 Vol. 3, pp 193-218. "Cytochrome P-450 Structure, Mechanism, and Biochemistry" Ortiz de Montellano, P. R., Ed. Plenum Press New York, 1986. 

M. Mure, S.A. Mills, J.P. Klinman, Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry 41 (2002) 9269-9278. 

S. Hirota, T. Iwamoto, S. Kishishita, T. Okajima, O. Yamauchi, K. Tanizawa, Spectroscopic observation of intermediates formed during the oxidative half-reaction of copper/topa quinone-containing phenylethylamine oxidase, Biochemistry 40 (2001) 15789-15796. 

Chander K. and P.C. Brookes (1993). Residual effects of zinc, copper and nickel in sewage sludge on microbial biomass in a sandy loam. Soil Biology and Biochemistry 25 1231-1239. 

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