Copper binding sites

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. 

Wang, J., Xu, G., Gonzales, V. et al. Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site. Neurobiol. Dis 10 128-138,2002. 

It is interesting to speculate why nitrite reductase has its type I coppers in domains 1, whereas in hCP the mononuclear copper binding sites are retained in the domains 2,4, and 6 where they are comparatively buried in the protein. One possible reason can be related to the difference in functions of the two proteins. NR has to interact with a relatively large pseudo-azurin macromolecule in order for electron transfer to take place,... 

A. G. Szabo, T. M. Stepanik, D. M. Wayner, and N. M. Young, Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study,... 

The copper-binding sites in copper-containing proteins are characterized by three distinct classes. In Type-1, or blue copper centers, the copper is coordinated to at least two imidazole nitrogens from two histidyl residues and one sulfur from a cysteinyl residue. Type-1 coppers have small copper hyperfine couplings and a strong visible absorption in the Cu(ll) state. Type-2 or non-blue copper... 

ANTIBODY-HAPTEN INTERACTIONS TYPE 1, 2, 3 COPPER BINDING SITES Type I dehydrogenase,... 

When the complete amino acid sequence of ceruloplasmin was determined, an internal threefold repeat suggested gene triplication (Ta-kahashi et al., 1983). Moreover, sequence similarity to the small blue copper domains suggested that there were at least two domains with blue copper-binding sites. Analysis of fragments of laccase sequence indicated that there might be a relationship of this to small blue proteins and ceruloplasmin as well (Ryden, 1988). 

Pinacolone, o-(diphenylphosphino)benzoyl-coordination chemistry, 401 Piperidine, IV-hydroxy-metal complexes, 797 pA a values azole ligands, 77 Plant roots amino acids, 962 carboxylic acids, 962 Plastocyanin copper binding site, 557 copper(II) complexes, 772 copper(II) site in, 770 Platinum, dichlorobis(benzonitrile)-IR spectrum, 264 Platinum, cis-dichlorodianunine-antitumor activity, 34, 979 Platinum, ethylenebis(triphenylphosphine)-reactions with 5,6-dimethyl-2,l,3-benzothiadiazole, 194 Platinum blue formation, 265 Platinum complexes acetylacetone reactions, 380 amides, 491 amidines... 

For the most part, adequate copper is received in diet and widespread human deficiencies do not occur, but deficiencies may arise because of antagonists. The metals Cd, Hg, Ag and Zn interfere with copper metabolism, probably by competing for copper-binding sites in proteins. Ascorbic acid depresses intestinal absorption of copper56 (in contrast to iron). Some proteins in the diet adversely affect utilization of copper. The sulfide ion is a well known inhibitor of copper absorption, since it forms copper(II) sulfide which is insoluble.56... 

Fig. 7. Inner sphere of the galactose oxidase copper-binding site. Geometric details of the ligand arrangement in the aquo complex are indicated in the figure. (Based on protein coordinates PDB ID IGOG.)...

Fig. 3. Comparison of the membrane topology of a CPx-type ATPase and a nonheavy metal ATPase. Shown are CopB of Enterococcus hirae and the Ca -ATPase of sarcoplasmic reticnlnm. Helices common to both types of ATPases are in gray and helices nniqne to one type of ATPase are in black. Key seqnence motifs are indicated in single-letter amino acid code. In the center of the hgnre, the approximate locations of the three cytoplasmic domains. A, P, and N, are indicated. MBD, metal-binding domain containing repeat metal-binding sites TGE, conserved site in transdnction domain (A) CPx, pntative copper-binding site DKTGT, phosphorylation site in domain P HP, motif of nnknown function, probably in domain N GDG, nucleotide-binding site residues in domain N.

Figure 8 shows a scheme of the reaction cycle of copper ATPases, assuming that they work by a mechanism analogous to that of Ca - or Na+, K+-ATPases. To pump ions, the enzyme must cycle between a state with a high-affinity copper-binding site accessible from only one side of the membrane and a low-affinity state in which the copper cavity is accessible from the other side of the membrane. The high- and low-affinity forms of P-type ATPases were initially named Ei and E2 by Racker (1980) and for many years these ATPases were called E]E2-ATPases, until they were renamed P-type by Pedersen and Carafoli (1987a). 

Fig. 4. Proposed regulation of catalytic activity and trafficking of ATP7A by the N-terminal putative copper-binding sites.

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