The electrochemistry of some copper-containing proteins and enzymes, viz. azurin, galactose oxidase, tyrosinase (catechol oxidase), and the "blue" multicopper oxidases (ascorbate oxidase, bilirubin oxidase, ceruloplasmin, laccase) is reviewed and discussed in conjunction with their basic biochemical and structural characteristics. It is shown that long-range electron transfer between these enzy...

Maize is susceptible to a number of diseases that can infect all plant organs and serve as constraint on cereal production. The reduction in production caused by disease estimated at an average 9.4%. Corn root rot contributes greatly the grain quality. main objective this work was review research maize determine susceptibility genotypes quantify inheritance resistance maize. methodology used co...

Preparation of cobalt(II) derivatives of type 1 copper proteins has been extended to include bean plastocyanin and azurin from Pseudomonas aeruginosa. Fluorescence quenching data suggest that Co(II) binds to the type 1 site of both apoplastocyanin and apoazurin. Electronic absorption spectral measurements have been made for cobalt(II)-stellacyanin, cobalt(II)-plastocyanin, and cobalt(II)-azurin...

S-Nitrosothiols are known as reagents for NO storage and transportation and as regulators in many physiological processes. Although the S-nitrosylation catalysed by haem proteins is well known, no direct evidence of S-nitrosylation in copper proteins has been reported. Here, we report reversible insertion of NO into a copper-thiolate bond in an engineered copper centre in Pseudomonas aeruginosa...

Understanding how the folding of proteins establishes their functional characteristics at the molecular level challenges both theorists and experimentalists. The simplest test beds for confronting this issue are provided by electron transfer proteins. The environment provided by the folded protein to the cofactor tunes the metal's electron transport capabilities as envisioned in the entatic hyp...

The reaction between a5RuH2O2+ (a is NH3) and Pseudomonas aeruginosa azurin at pH 7, followed by oxidation, yields a5Ru(His-83)3+-azurin(Cu2+) as the major product. Spectroscopic measurements (UV-visible, CD, EPR, and resonance Raman) indicate that the native structure is maintained in the modified protein. The site of ruthenium binding (His-83) was identified by peptide mapping. The a5RuHis/Cu...

The mutations W48F, Y72F, H83Q, Q107H, Y108W were carried out stepwise using Invitrogene primers and a QuickChange® kit (Stratagene). The modified DNA plasmid (verified sequencing) was incorporated into BL21(DE3) E. Coli (Novagene). Bacteria were grown in a standard LB broth to an optical density of ~2. After harvesting, the cells were subjected to lysis by the osmotic shock method. The peripla...

This paper reports on the optimization of conditions for the overproduction and isolation of two recombinant copper metalloproteins, originally encoded on the chromosome of the dentrifying soil bacterium Alcaligenes xylosoxidans, in the heterologous host Escherichia coli. The trimeric enzyme nitrite reductase (NiR) contains both type-1 and type-2 Cu centres, whilst its putative redox partner, a...

A stopped-flow investigation of the electron-transfer reaction between oxidized azurin and reduced Pseudomonas aeruginosa cytochrome c-551 oxidase and between reduced azurin and oxidized Ps. aeruginosa cytochrome c-551 oxidase was performed. Electrons leave and enter the oxidase molecule via its haem c component, with the oxidation and reduction of the haem d1 occurring by internal electron tra...

Fluorescence depolarization of the exposed tryptophanyl residue in the peptide melittin and the buried tryptophanyl residue in the protein azurin (from the bacteria Pseudomonos aeruginoso) was measured with subpicosecond resolution at various excitation and emission wavelengths. A short time component was found in both the fluorescence decay and fluorescence anisotropy decay for the tryptophany...