we have evaluated the nmr shielding tensors for active site of oxidized ayurin azurin is classified to atype i copper protein with et functionality. we have computed nmr shielding tensor at .133lyp and idlevels by usum 6-3ig basis set in the gas phase and in different solvents such as water, hmso,nitromethane, methanol, ethanol, acetone ,dicholoroethane. these solvents represent a wide range of...

Nitrosocyanin (NC) is a mononuclear red copper protein isolated from the ammonia oxidizing bacterium Nitrosomonas europaea. Although NC exhibits some sequence homology to classic blue copper proteins, its spectroscopic and electrochemical properties are drastically different. The 1.65 A resolution crystal structure of oxidized NC reveals an unprecedented trimer of single domain cupredoxins. Eac...

We have evaluated the NMR shielding tensors for active site of oxidized ayurin Azurin is classified to atype I copper protein with ET functionality. We have computed NMR shielding tensor at .133LYP and IDlevels by usum 6-3IG basis set in the gas phase and in different solvents such as water, HMSO,Nitromethane, methanol, ethanol, acetone ,dicholoroethane. These solvents represent a wide range of...

The objectives of this and the following paper are to identify commonalities and disparities of the extended environment of mononuclear metal sites centering on Cu, Fe, Mn, and Zn. The extended environment of a metal site within a protein embodies at least three layers: the metal core, the ligand group, and the second shell, which is defined here to consist of all residues distant less than 3.5...

a series of schiff bases of ni(ii) and cu(ii) using acetylacetone (acac), salicylaldehyde (sal), ethylenediamine (en), and o-phenylendiarnine (dabe) were prepared and characterized. the electronic spectra of some copper chelates in various organic solvents depend strongly on the solvent used and the d-d band of cu(ii) shifts to red with the increase of the donor number (dn) of solvent. the colo...

When grown on methylamine as a sole carbon source, Paracoccus denitrificans synthesizes a Type I blue copper protein which mediates electron transfer between methylamine dehydrogenase and cytochrome c. This blue copper protein does not serve as an electron acceptor for methanol dehydrogenase and is not synthesized by cells grown on methanol or succinate. The blue copper protein and methylamine ...

The Cu(II)- and Co(II)-binding properties of two peptides, designed on the basis of the active site sequence and structure of the blue copper protein plastocyanin, are explored. Peptide BCP-A, Ac-Trp-(Gly)(3)-Ser-Tyr-Cys-Ser-Pro-His-Gln-Gly-Ala-Gly-Met-(Gly )(3)-His-(Gly)(2)-Lys-CONH(2), conserves the Cu-binding loop of plastocyanin containing three of the four copper ligands and has a flexible...

A series of Schiff Bases of Ni(II) and Cu(II) using acetylacetone (acac), salicylaldehyde (sal), ethylenediamine (en), and o-phenylendiarnine (dabe) were prepared and characterized. The electronic spectra of some copper chelates in various organic solvents depend strongly on the solvent used and the d-d band of Cu(II) shifts to red with the increase of the Donor Number (DN) of solvent. The ...

1. A procedure is described for isolating a copper protein from horse liver in pure form, in a state that appears to be crystalline. 2. This copper protein is colored blue-green, and its copper content varied between 0.3 and 0.4 per cent. No indication of any catalytic properties was obtained in the limited number of tests made. Because of its variable copper content, the protein may function f...

Copper induces a red pigmentation in cells of the bacterium Myxococcus xanthus when they are incubated in the dark, at suboptimal growth conditions. The colouration results from the accumulation of carotenoids, as demonstrated by chemical analysis, and by the lack of a copper effect on M. xanthus mutants affected in known structural genes for carotenoid synthesis. None of several other metals o...