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Metalloprotein Electronics
Published in Sergey Edward Lyshevski, Nano and Molecular Electronics Handbook, 2018
Andrea Alessandrini, Paolo Facci
Azurin from Pseudomonas aeruginosa is a soluble protein (molecular mass 14600) involved in the oxidative phosphorylation of its expressing bacterium. It is believed to accomplish the function of shuttling electrons between two molecular partners, cytochrome c551 and nitrite reductase, which act as the primary donor and acceptor, respectively [18]. Its functional behavior is guaranteed by the reversible oxidation of Cu+1 to Cu+2. The peculiar electronic properties of this molecule are connected with the special structural features of its redox active site. Indeed, it contains a copper ion ligated to five aminoacids (two hystidines and a cysteine strongly bound to copper, and two weaker axial ligands: a methionine and a main chain carbonyl oxygen) [19] according to a peculiar ligand-field symmetry that provides the center with unusual spectroscopic and electrochemical properties. Among them, an intense electron absorption band at 628 nm (due to the S(Cys)-Cu bonding to anti-bonding transition), a small hyperfine splitting in the electron paramagnetic spectrum [20] and an unusually large standard potential (+116mV versus SCE) [21] in comparison to the Cu(II/I) aqua couple (–89 mV versus SCE) [22].
Heterologous expression of azurin from Pseudomonas aeruginosa in the yeast Pichia pastoris
Published in Preparative Biochemistry & Biotechnology, 2021
Yagmur Unver, Busra Sensoy Gun, Melek Acar, Seyda Yildiz
The secondary metabolites are used in developing new chemotherapeutics and drugs. Azurin, which is a secondary metabolite can be used as a potential anticancer agent because it induced the death of cancer cells and inhibited their growth. Therefore, the usage of recombinant azurin protein as a potential anticancer agent should be important for cancer therapy. In this study, the expression of the azurin gene was carried out for the first time in P. pastoris. Furthermore, the effective expression of therapeutic azurin protein was obtained by screening multicopy azurin recombinants. In the next studies, process optimization such as pH, temperature, incubation time and methanol concentration, purification of this protein, and determination of its therapeutic effects on breast cancer will be focused on.
Heterologous expression of azurin from Pseudomonas aeruginosa in food-grade Lactococcus lactis
Published in Preparative Biochemistry and Biotechnology, 2019
Azurin is a bacterial protein, which is produced by P. aeruginosa. It has a low molecular weight (14 kDa) consisting of 128 amino acids and is localized in the periplasmic gap of P. aeruginosa.[7,8] Azurin is known as an anticancer bacteriocin. Bacteriocins are antibacterial proteins produced by bacteria that kill or inhibit the growth of other similar or closely related bacteria. They are used to improve food safety and quality.[9]