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Journal articles on the topic 'Azurin protein'

Author: Grafiati

Published: 6 September 2023

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1

Yamada, Tohru, Masatoshi Goto, Vasu Punj, Olga Zaborina, Kazuhide Kimbara, T. K. Das Gupta, and A. M. Chakrabarty. "The Bacterial Redox Protein Azurin Induces Apoptosis in J774 Macrophages through Complex Formation and Stabilization of the Tumor Suppressor Protein p53." Infection and Immunity 70, no. 12 (December 2002): 7054–62. http://dx.doi.org/10.1128/iai.70.12.7054-7062.2002.

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ABSTRACT Two redox proteins, azurin and cytochrome c 551 elaborated by Pseudomonas aeruginosa, demonstrate significant cytotoxic activity towards macrophages. Azurin can enter macrophages, localize in the cytosol and nuclear fractions, and induce apoptosis. Two redox-negative mutants of azurin have less cytotoxicity than does wild-type (wt) azurin. Azurin has been shown to form a complex with the tumor suppressor protein p53, a known inducer of apoptosis, thereby stabilizing it and enhancing its intracellular level. A higher level of reactive oxygen species (ROS), generated during treatment of macrophages with wt azurin, correlates with its cytotoxicity. Treatment with some ROS-removing antioxidants greatly reduces azurin-mediated cytotoxicity, thus demonstrating a novel virulence property of this bacterial redox protein.

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2

Aslam, Shakira, Hafiz Muzzammel Rehman, Muhammad Zeeshan Sarwar, Ajaz Ahmad, Nadeem Ahmed, Muhammad Imran Amirzada, Hafiz Muhammad Rehman, Humaira Yasmin, Tariq Nadeem, and Hamid Bashir. "Computational Modeling, High-Level Soluble Expression and In Vitro Cytotoxicity Assessment of Recombinant Pseudomonas aeruginosa Azurin: A Promising Anti-Cancer Therapeutic Candidate." Pharmaceutics 15, no. 7 (June 26, 2023): 1825. http://dx.doi.org/10.3390/pharmaceutics15071825.

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Azurin is a natural protein produced by Pseudomonas aeruginosa that exhibits potential anti-tumor, anti-HIV, and anti-parasitic properties. The current study aimed to investigate the potential of azurin protein against breast cancer using both in silico and in vitro analyses. The amino acid sequence of Azurin was used to predict its secondary and tertiary structures, along with its physicochemical properties, using online software. The resulting structure was validated and confirmed using Ramachandran plots and ERRAT2. The mature azurin protein comprises 128 amino acids, and the top-ranked structure obtained from I-TASSER was shown to have a molecular weight of 14 kDa and a quality factor of 100% by ERRAT2, with 87.4% of residues in the favored region of the Ramachandran plot. Docking and simulation studies of azurin protein were conducted using HDOCK and Desmond servers, respectively. The resulting analysis revealed that Azurin docked against p53 and EphB2 receptors demonstrated maximum binding affinity, indicating its potential to cause apoptosis. The recombinant azurin gene was successfully cloned and expressed in a BL21 (DE3) strain using a pET20b expression vector under the control of the pelB ladder, followed by IPTG induction. The azurin protein was purified to high levels using affinity chromatography, yielding 70 mg/L. In vitro cytotoxicity assay was performed using MCF-7 cells, revealing the significant cytotoxicity of the azurin protein to be 105 µg/mL. These findings highlight the potential of azurin protein as an anticancer drug candidate.

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3

Valli S, Abiraami, and Mythili T. "BIOINFORMATIC STUDY OF AN ANTITUMOR PROTEIN, AZURIN." Asian Journal of Pharmaceutical and Clinical Research 11, no. 6 (June 7, 2018): 169. http://dx.doi.org/10.22159/ajpcr.2018.v11i6.23339.

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Objective: The main objective of this study is to analyze the structure and function of an antitumor protein, azurin, thereby giving validation to the protein structure and existing physicochemical properties in the anticancer protein which are responsible for the anticancer activity.Methods: Protein sequence analysis was done using Basic Local Alignment Search Tool (BLAST) with ten different randomly selected species of Pseudomonas obtained from GenBank. The physicochemical properties, prediction of secondary structure, identification of motifs and domains, three-dimensional (3-D) structure of the antitumor protein, validation through Ramachandran plot, multiple sequence alignment (MSA), and phylogenetic analysis were studied and functional property was confirmed through in silico docking.Results: The similarity search (BLAST-P analysis) for the primary sequence from GenBank carried out showed 86% similarity to the second sequence, azurin (Pseudomonas nitroreducens). The ProtParam, ExPASy tool server indicated the presence of essential physicochemical properties in azurin. Secondary structure prediction revealed random coil, extended strand, alpha helix, and beta turn. The study on domains indicated the presence of one domain in azurin responsible for the anticancer activity. The 3-D structural analysis revealed azurin as metalloprotein, of length-128, and polymer-1 with α-helices, β-sheets, and β-barrels. The validation carried out through Ramachandran plot showed the presence of two outliers (phi and psi). The biological relationship between the input sequences was studied through MSA and phylogenetic analysis. Further, azurin docked against the target protein (p53 tumor suppressor) showed the maximum binding affinity confirming its functional property of causing apoptosis.Conclusion: All the properties analyzed in the present study revealed that the azurin protein can act as a very good anticancer agent, and through the phylogenetic analysis, it was identified that Pseudomonas nitroreducens was closely related to the test organism Pseudomonas aeruginosa.

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4

Signorelli, Sara, Salvatore Cannistraro, and Anna Rita Bizzarri. "Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin." International Journal of Molecular Sciences 20, no. 12 (June 24, 2019): 3078. http://dx.doi.org/10.3390/ijms20123078.

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Raman spectroscopy, which is a suitable tool to elucidate the structural properties of intrinsically disordered proteins, was applied to investigate the changes in both the structure and the conformational heterogeneity of the DNA-binding domain (DBD) belonging to the intrinsically disordered protein p53 upon its binding to Azurin, an electron-transfer anticancer protein from Pseudomonas aeruginosa. The Raman spectra of the DBD and Azurin, isolated in solution or forming a complex, were analyzed by a combined analysis based on peak inspection, band convolution, and principal component analysis (PCA). In particular, our attention was focused on the Raman peaks of Tyrosine and Tryptophan residues, which are diagnostic markers of protein side chain environment, and on the Amide I band, of which the deconvolution allows us to extract information about α-helix, β-sheet, and random coil contents. The results show an increase of the secondary structure content of DBD concomitantly with a decrease of its conformational heterogeneity upon its binding to Azurin. These findings suggest an Azurin-induced conformational change of DBD structure with possible implications for p53 functionality.

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5

Naguleswaran, Arunasalam, Arsenio M. Fialho, Anita Chaudhari, Chang Soo Hong, Ananda M. Chakrabarty, and William J. Sullivan. "Azurin-Like Protein Blocks Invasion of Toxoplasma gondii through Potential Interactions with Parasite Surface Antigen SAG1." Antimicrobial Agents and Chemotherapy 52, no. 2 (December 10, 2007): 402–8. http://dx.doi.org/10.1128/aac.01005-07.

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ABSTRACT Some pathogenic bacteria produce factors that have evolved a capacity to neutralize competing microbes. The cupredoxin family protein azurin, produced by Pseudomonas aeruginosa, exhibits a remarkable ability to impede invasion of a number of diverse intracellular pathogens, including the human AIDS virus human immunodeficiency virus type 1 and the protozoan parasite Plasmodium falciparum (which causes malaria). Here we report that azurin and an azurin-like protein (Laz) from gonococci/meningococci have activity against Toxoplasma, an apicomplexan parasite that causes opportunistic infection in immunocompromised individuals. We demonstrate that the mechanism of action for Laz involves interfering with the ability of Toxoplasma to adhere to host cells. Computer structural analysis reveals that azurin shares structural features with the predominant surface antigen SAG1, which is known to play an important role in parasite attachment. Interestingly, azurin also has structural similarities to a monoclonal antibody to SAG1. Surface plasmon resonance binding studies validate that SAG1 interacts strongly with Laz and, to lesser extent, azurin. Moreover, Toxoplasma mutants lacking SAG1 are not as susceptible to the growth-inhibitory effects of Laz. Collectively, our data show that Toxoplasma adhesion can be significantly impaired by Laz, and to some extent by azurin, via interactions with SAG1. These observations indicate that Laz can serve as an important tool in the study of host-pathogen interactions and is worthy of further study for development into potential therapeutic agents.

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6

Gammuto, Leandro, Carolina Chiellini, Marta Iozzo, Renato Fani, and Giulio Petroni. "The Azurin Coding Gene: Origin and Phylogenetic Distribution." Microorganisms 10, no. 1 (December 22, 2021): 9. http://dx.doi.org/10.3390/microorganisms10010009.

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Azurin is a bacterial-derived cupredoxin, which is mainly involved in electron transport reactions. Interest in azurin protein has risen in recent years due to its anticancer activity and its possible applications in anticancer therapies. Nevertheless, the attention of the scientific community only focused on the azurin protein found in Pseudomonas aeruginosa (Proteobacteria, Gammaproteobacteria). In this work, we performed the first comprehensive screening of all the bacterial genomes available in online repositories to assess azurin distribution in the three domains of life. The Azurin coding gene was not detected in the domains Archaea and Eucarya, whereas it was detected in phyla other than Proteobacteria, such as Bacteroidetes, Verrucomicrobia and Chloroflexi, and a phylogenetic analysis of the retrieved sequences was performed. Observed patchy distribution and phylogenetic data suggest that once it appeared in the bacterial domain, the azurin coding gene was lost in several bacterial phyla and/or anciently horizontally transferred between different phyla, even though a vertical inheritance appeared to be the major force driving the transmission of this gene. Interestingly, a shared conserved domain has been found among azurin members of all the investigated phyla. This domain is already known in P. aeruginosa as p28 domain and its importance for azurin anticancer activity has been widely explored. These findings may open a new and intriguing perspective in deciphering the azurin anticancer mechanisms and to develop new tools for treating cancer diseases.

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7

Ambler, R. P., and J. Tobari. "Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J." Biochemical Journal 261, no. 2 (July 15, 1989): 495–99. http://dx.doi.org/10.1042/bj2610495.

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Methylomonas J is an obligate methylotroph although it is unable to grow on methane. Like Pseudomonas AM1, it produces two blue copper proteins when growing on methylamine, one of which is the recipient of electrons from the methylamine dehydrogenase. When grown on methanol, only the other blue copper protein is produced. We have determined the amino acid sequences of these blue copper proteins, and show that they are both true azurins. The sequences are clearly homologous to those of the proteins characterized from fluorescent pseudomonads and various species of Alcaligenes, and can be aligned with them and with each other without the need to postulate any internal insertions or deletions in the sequences. The iso-1 azurin, the one produced during both methanol and methylamine growth, shows 59-65% identity with these other azurins, whereas the iso-2 protein shows only 47-53% identity. The proteins show 52% identity with each other. The two functionally equivalent blue copper proteins from Pseudomonas AM1 belong to two sequence classes that are quite distinct from the true azurins. Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50151 (23 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257, 5.

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8

Fialho, Arsenio M., Prabhakar Salunkhe, Sunil Manna, Sidharth Mahali, and Ananda M. Chakrabarty. "Glioblastoma Multiforme: Novel Therapeutic Approaches." ISRN Neurology 2012 (February 8, 2012): 1–10. http://dx.doi.org/10.5402/2012/642345.

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The current therapy for glioblastoma multiforme involves total surgical resection followed by combination of radiation therapy and temozolomide. Unfortunately, the efficacy for such current therapy is limited, and newer approaches are sorely needed to treat this deadly disease. We have recently described the isolation of bacterial proteins and peptides with anticancer activity. In phase I human clinical trials, one such peptide, p28, derived from a bacterial protein azurin, showed partial and complete regression of tumors in several patients among 15 advanced-stage cancer patients with refractory metastatic tumors where the tumors were no longer responsive to current conventional drugs. An azurin-like protein called Laz derived from Neisseria meningitides demonstrates efficient entry and high cytotoxicity towards glioblastoma cells. Laz differs from azurin in having an additional 39-amino-acid peptide called an H.8 epitope, which allows entry and high cytotoxicity towards glioblastoma cells. Since p28 has been shown to have very little toxicity and high anti-tumor activity in advanced-stage cancer patients, it will be worthwhile to explore the use of H.8-p28, H.8-azurin, and Laz in toxicity studies and glioblastoma therapy in preclinical and human clinical trials.

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9

Kretchmer, Joshua S., Nicholas Boekelheide, Jeffrey J. Warren, Jay R. Winkler, Harry B. Gray, and Thomas F. Miller. "Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein." Proceedings of the National Academy of Sciences 115, no. 24 (May 29, 2018): 6129–34. http://dx.doi.org/10.1073/pnas.1805719115.

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We combine experimental and computational methods to address the anomalous kinetics of long-range electron transfer (ET) in mutants of Pseudomonas aeruginosa azurin. ET rates and driving forces for wild type (WT) and three N47X mutants (X = L, S, and D) of Ru(2,2′-bipyridine)2 (imidazole)(His83) azurin are reported. An enhanced ET rate for the N47L mutant suggests either an increase of the donor–acceptor (DA) electronic coupling or a decrease in the reorganization energy for the reaction. The underlying atomistic features are investigated using a recently developed nonadiabatic molecular dynamics method to simulate ET in each of the azurin mutants, revealing unexpected aspects of DA electronic coupling. In particular, WT azurin and all studied mutants exhibit more DA compression during ET (>2 Å) than previously recognized. Moreover, it is found that DA compression involves an extended network of hydrogen bonds, the fluctuations of which gate the ET reaction, such that DA compression is facilitated by transiently rupturing hydrogen bonds. It is found that the N47L mutant intrinsically disrupts this hydrogen-bond network, enabling particularly facile DA compression. This work, which reveals the surprisingly fluctional nature of ET in azurin, suggests that hydrogen-bond networks can modulate the efficiency of long-range biological ET.

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10

Ortega, Vilhena, Zotti, Díez-Pérez, Cuevas, and Pérez. "Tuning Structure and Dynamics of Blue Copper Azurin Junctions via Single Amino-Acid Mutations." Biomolecules 9, no. 10 (October 15, 2019): 611. http://dx.doi.org/10.3390/biom9100611.

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In the growing field of biomolecular electronics, blue-copper Azurin stands out as one of the most widely studied protein in single-molecule contacts. Interestingly, despite the paramount importance of the structure/dynamics of molecular contacts in their transport properties, these factors remain largely unexplored from the theoretical point of view in the context of single Azurin junctions. Here we address this issue using all-atom Molecular Dynamics (MD) of Pseudomonas Aeruginosa Azurin adsorbed to a Au(111) substrate. In particular, we focus on the structure and dynamics of the free/adsorbed protein and how these properties are altered upon single-point mutations. The results revealed that wild-type Azurin adsorbs on Au(111) along two well defined configurations: one tethered via cysteine groups and the other via the hydrophobic pocket surrounding the Cu 2 + . Surprisingly, our simulations revealed that single amino-acid mutations gave rise to a quenching of protein vibrations ultimately resulting in its overall stiffening. Given the role of amino-acid vibrations and reorientation in the dehydration process at the protein-water-substrate interface, we suggest that this might have an effect on the adsorption process of the mutant, giving rise to new adsorption configurations.

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11

Karlsson, B. Göran, Margareta Nordling, Torbjörn Pascher, Li-Chu Tsai, Lennart Sjölin, and Lennart G. Lundberg. "Cassette mutagenesis of Met121 in azurin from Pseudomonas aeruginosa." "Protein Engineering, Design and Selection" 4, no. 3 (1991): 343–49. http://dx.doi.org/10.1093/protein/4.3.343.

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12

Punj, Vasu, Rachna Sharma, Olga Zaborina, and A. M. Chakrabarty. "Energy-Generating Enzymes of Burkholderia cepacia and Their Interactions with Macrophages." Journal of Bacteriology 185, no. 10 (May 15, 2003): 3167–78. http://dx.doi.org/10.1128/jb.185.10.3167-3178.2003.

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ABSTRACT We previously demonstrated that several clinical and environmental isolates of Burkholderia cepacia secreted ATP-utilizing enzymes to the medium; the secretion of these enzymes by cystic fibrosis lung isolate strain 38 was shown to be greatly enhanced in the presence of α2-macroglobulin. Fractionation of the growth medium of cystic fibrosis isolate strain 71 belonging to genomovar I demonstrated the presence of two additional proteins, homologues of Pseudomonas aeruginosa azurin and cytochrome c 551, which are normally involved in electron transfer during denitrification. A Q-Sepharose column flowthrough fraction of the growth medium of B. cepacia strain 71 enriched with the azurin and cytochrome c 551 homologues triggered apoptosis in macrophages and mast cells, leading to their death. Incubation of the Q-Sepharose column flowthrough fraction with antiazurin and anti-cytochrome c 551 antibodies greatly reduced cell death. We cloned and hyperexpressed a gene from B. cepacia strain 71 that encodes the homologue of P. aeruginosa azurin. Such azurin homologues were detected in the growth medium of several strains belonging to genomovars I, III, and VI but not in the growth medium of strains belonging to other genomovars. The growth medium of the strains that elaborated the azurin homologue had high cytotoxicity towards macrophages. Purified azurin homologue was shown to induce apoptosis in macrophages in a caspase-dependent manner and was localized in both the cytosol and nucleus when incubated with or microinjected into macrophages. This is an interesting example of the interaction of a bacterial protein normally involved in cellular energetics with macrophages to effect their cell death.

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Nguyen, Chuong, and Van Duy Nguyen. "Discovery of Azurin-Like Anticancer Bacteriocins from Human Gut Microbiome through Homology Modeling and Molecular Docking against the Tumor Suppressor p53." BioMed Research International 2016 (2016): 1–12. http://dx.doi.org/10.1155/2016/8490482.

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Azurin fromPseudomonas aeruginosais known anticancer bacteriocin, which can specifically penetrate human cancer cells and induce apoptosis. We hypothesized that pathogenic and commensal bacteria with long term residence in human body can produce azurin-like bacteriocins as a weapon against the invasion of cancers. In our previous work, putative bacteriocins have been screened from complete genomes of 66 dominant bacteria species in human gut microbiota and subsequently characterized by subjecting them as functional annotation algorithms with azurin as control. We have qualitatively predicted 14 putative bacteriocins that possessed functional properties very similar to those of azurin. In this work, we perform a number of quantitative and structure-based analyses including hydrophobic percentage calculation, structural modeling, and molecular docking study of bacteriocins of interest against protein p53, a cancer target. Finally, we have identified 8 putative bacteriocins that bind p53 in a same manner as p28-azurin and azurin, in which 3 peptides (p1seq16, p2seq20, and p3seq24) shared with our previous study and 5 novel ones (p1seq09, p2seq05, p2seq08, p3seq02, and p3seq17) discovered in the first time. These bacteriocins are suggested for furtherin vitrotests in different neoplastic line cells.

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Yamada, T., R. Mehta, D. Majumdar, A. M. Chakrabarty, and T. K. Das Gupta. "Azurin, highly potent and selective anticancer agent for breast cancer." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 13106. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.13106.

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13106 Background: The use of live or attenuated pathogenic bacteria in the treatment of cancer dates back to the late nineteen hundreds when William B. Coley first reported that inducing Streptococcal infection resulted in tumor regression. However, the hazards of using live bacteria are obvious. Similarly, the results of using attenuated bacteria have been spotty and enthusiasm for it has waxed and waned. Recently, we have shown that redox protein azurin (14 kDa) secreted by an opportunistic pathogen, Pseudomonas aeruginosa, is not only cytotoxic to cancer cells in vitro but also produces tumor regression in athymic mice without producing any toxicity (PNAS, 99, 14098–14103, 2002; Science’s STKE, 158, tw416, 2002). Methods: In this study, we show the effect of 1mg/kg of azurin injected i.p. starting 72 hours after inoculation of 5x107 MCF-7 breast cancer cells in estradiol pretreated nude mice for 28 days (n = 20, control = 10, azurin-treated = 10). Results: Univariate analysis of the data showed the difference in tumor growth rates between control animals and azurin-treated animals was significant. For instance, 22 days after the start of treatment, the mean tumor volume in azurin-treated animals was only 22% of the mean tumor volume in the control mice (i.e., 0.0267 cm3 + 0.124 cm3 respectively, P = 0.0179 Kruskal-Wallis test). At the end of the experiment on the 29th day there was a reduction in the tumor volume by 85% in the treated group. We used a multivariate model, where the tumor growth over time was taken to be exponential with coefficients that were subject specific mixed effect (For control, tumor volumes = exp (−4.23 + 0.06 time) while for the treated group it was tumor volume = exp (−4.23 + 0.03 time)). The difference is statistically significant (P = 0.0456). Taken together, this in vivo data shows azurin exerts an inhibitory effect in the growth and progression of MCF-7 tumor xenotransplants. During the 28 days of treatment, treated animals did not show any sign of toxicity. Conclusions: Bacterial redox protein azurin can be explored as a novel therapeutic agent for treatment of breast cancer. Recently, we have prepared a truncated version of azurin which has 28 amino acids. It appers that this chemically synthesized peptide (2.8 kDa) has similar properties as azurin. No significant financial relationships to disclose.

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Ghasemi-Dehkordi, Payam, Abbas Doosti, and Mohammad-Saeid Jami. "The effects of pBudCE4.1-azurin-MAM-A recombinant vector on IL-2, IL-6, IL-7, and IL-10 expressions in laboratory mice." Journal of Shahrekord University of Medical Sciences 22, no. 1 (February 28, 2020): 38–45. http://dx.doi.org/10.34172/jsums.2020.07.

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Background and aims: Breast cancer is one of the most common types of malignancy in women with morbidity and mortality (15.0%) in the world. The antitumor activity of azurin protein produced by Pseudomonas aeruginosa has been described before. Mammaglobin-A (MAM-A) protein is especially expressed in 40%-80% of breast cancer types and this protein is a very specific molecular marker for stimulating the immune system. Accordingly, this study investigated the effects of pBudCE4.1-azurin-MAM-A recombinant vector on the induction of the immune system in laboratory mice by the real-time polymerase chain reaction (PCR) method. Methods: The pBudCE4.1-azurin-MAM-A recombinant and empty vectors were purchased and then separately transformed into Escherichia coli for multiplying. Next, each plasmid was extracted and the accuracy of transformation was confirmed by the PCR. These recombinant and empty (control) vectors were separately infused into the thigh muscle of the animals and the healthy group was infused with phosphatebuffered saline. The infusion sites, blood specimens, as well as the serum of the animals were collected and examined by serological and molecular tests. Results: Molecular and serological studies showed that the serum and expression levels of IL-2, IL-6, IL-7, and IL-10 in infused mice with pBudCE4.1-azurin-MAM-A recombinant vector significantly increased compared to healthy animals and injected mice with an empty vector (P<0.05). Conclusion: In general, the findings revealed that the pBudCE4.1-azurin-MAM-A recombinant vector can stimulate the immune system of the mouse by an increase in the expression levels of IL-2, IL-6, IL-7, and IL-10. Thus, it would be better to examine the effects of this recombinant vector as a DNA vaccine on the prevention and treatment of breast cancer.

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Naro, Fabio, Maria G. Tordi, Giorgio M. Giacometti, Francesco Tomei, Anna M. Timperio, and Lello Zolla. "Metal Binding to Pseudomonas aeruginosa Azurin: a Kinetic Investigation." Zeitschrift für Naturforschung C 55, no. 5-6 (June 1, 2000): 347–54. http://dx.doi.org/10.1515/znc-2000-5-609.

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The interaction between azurin from Pseudomonas aeruginosa and Ag(I), Cu(II), Hg(II), was investigated as a function of protein state, i.e. apo-, reduced and oxidised azurin. Two different metal binding sites, characterized by two different spectroscopic absorbancies, were detected: one is accessible to Ag(I) and Cu(II) but not to Hg(II); the other one binds Ag(I) and Hg(II) but not copper. When added in stoichiometric amount, Ag(I) shows high affinity for the redox center of apo-azurin, to which it probably binds by the -SH group of Cys112; it can displace Cu(I) from reducedazurin, while it does not bind to the redox center of oxidizedazurin. Kinetic experiments show that Ag(I) binding to the reducedform is four times faster than binding to the apo-form. This result suggests that metal binding requires a conformational rearrangement of the active site of the azurin. Interaction of A g(I) or Hg(II) ions to the second metal binding site, induces typical changes of UV spectrum and quenching of fluorescence emission.

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Pradhan, Biswajit, Christopher Engelhard, Sebastiaan Van Mulken, Xueyan Miao, Gerard W. Canters, and Michel Orrit. "Single electron transfer events and dynamical heterogeneity in the small protein azurin from Pseudomonas aeruginosa." Chemical Science 11, no. 3 (2020): 763–71. http://dx.doi.org/10.1039/c9sc05405g.

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Ho, Man Yi, Sarah A. Goodchild, Pedro Estrela, Daping Chu, and Piero Migliorato. "Switching of electrochemical characteristics of redox protein upon specific biomolecular interactions." Analyst 139, no. 23 (2014): 6118–21. http://dx.doi.org/10.1039/c4an01591f.

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Label-free protein sensing platform based on a simplified and standardized immobilization process with Azurin redox self-assembled monolayer is fabricated. A significant change in the electrochemical characteristics of the assay upon specific interaction with target molecules is observed.

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Sharma, Mukesh Kumar. "Annotated protein network analysis linking oral diseases." Bioinformation 18, no. 8 (August 31, 2022): 724–29. http://dx.doi.org/10.6026/97320630018724.

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Oral cancer is becoming more common, and it threatens to be a serious worldwide medical issue. Hence, it is of interest to elucidate the networks between proteins and biologically active compounds, as well as their functional annotations, and cell signaling pathways. The online STRING software was used to create a molecular genetics interaction network named AZURIN on oral bacterial proteins. We also used the cystoscope software to identify 11 nodes and 16 edges with an average node order of 2.91. Thus, we document data on the interaction of protein networks with other proteins for identifying potential therapeutic drug candidates linked to oral disease.

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de Jongh, Thyra E., Miguel Prudencio, Marcellus Ubbink, and Gerard W. Canters. "Modelling protein-protein electron transfer in cross-linked dimers of azurin." Journal of Inorganic Biochemistry 96, no. 1 (July 2003): 161. http://dx.doi.org/10.1016/s0162-0134(03)80663-3.

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Trinh, Dinh Kha, Thi Thao Nguyen, Thi Huyen La, Thi Thu Huyen Nguyen, and Thi Tuyen Do. "Cloning, expression and anticancer activity of azurin from Pseudomonas aeruginosa VTCC-B-657." Research Journal of Biotechnology 18, no. 1 (December 15, 2022): 1–6. http://dx.doi.org/10.25303/1801rjbt01006.

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Azurin, a small molecular weight protein produced by Pseudomonas aeruginosa and several gram-negative bacteria has received considerable attention because of its potential anti-parasitic, anti-viral and anti-cancer activity. In this study, 437 bp-gene of azurin was amplified and cloned from Pseudomonas aeruginosa VTCC-B-657. This gene was then inserted into the PET22b+ vector and the recombinant plasmid was introduced into Escherichia coli BL21(DE3) by chemical methods. The recombinant strain was checked by polymerase chain reaction method and sequencing analysis. Next, the recombinant azurin (r-Azu) was expressed and purified by Ni2+-ProBondTM resin column. The molecular mass of purified r-Azu was 16 kDa when determined by SDS-PAGE and was 13.88 kDa when determined by LC/MS. Interestingly, the purified r-Azu showed cytostatic activity only on breast cancer cell lines (MCF-7 and MDA with IC50 of 25.4 and 29.25 μg/ml respectively) but not on normal cells. These results suggest that r-Azu would be a potential candidate for anticancer drugs and deserves further study.

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M. Fialho, Arsenio, Nuno Bernardes, and Ananda M Chakrabarty. "Exploring the anticancer potential of the bacterial protein azurin." AIMS Microbiology 2, no. 3 (2016): 292–303. http://dx.doi.org/10.3934/microbiol.2016.3.292.

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23

Yagati, Ajay Kumar, Sang-Uk Kim, Junhong Min, and Jeong-Woo Choi. "Multi-bit biomemory consisting of recombinant protein variants, azurin." Biosensors and Bioelectronics 24, no. 5 (January 2009): 1503–7. http://dx.doi.org/10.1016/j.bios.2008.07.080.

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Kim, Sang-Uk, Ajay Kumar Yagati, Junhong Min, and Jeong-Woo Choi. "Nanoscale protein-based memory device composed of recombinant azurin." Biomaterials 31, no. 6 (February 2010): 1293–98. http://dx.doi.org/10.1016/j.biomaterials.2009.10.032.

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25

Yamada, T., M. Goto, V. Punj, O. Zaborina, M. L. Chen, K. Kimbara, D. Majumdar, E. Cunningham, T. K. Das Gupta, and A. M. Chakrabarty. "Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer." Proceedings of the National Academy of Sciences 99, no. 22 (October 22, 2002): 14098–103. http://dx.doi.org/10.1073/pnas.222539699.

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Zhang, Yunlei, Youming Zhang, Liqiu Xia, Xiangli Zhang, Xuezhi Ding, Fu Yan, and Feng Wu. "Escherichia coli Nissle 1917 Targets and Restrains Mouse B16 Melanoma and 4T1 Breast Tumors through Expression of Azurin Protein." Applied and Environmental Microbiology 78, no. 21 (August 24, 2012): 7603–10. http://dx.doi.org/10.1128/aem.01390-12.

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ABSTRACTMany studies have demonstrated that intravenously administered bacteria can target and proliferate in solid tumors and then quickly be released from other organs. Here, we employed the tumor-targeting property ofEscherichia coliNissle 1917 to inhibit mouse B16 melanoma and 4T1 breast tumors through the expression of azurin protein. For this purpose, recombinant azurin-expressingE. coliNissle 1917 was developed. The levels ofin vitroandin vivoazurin secretion in the engineered bacterium were determined by immunochemistry. Our results demonstrated that B16 melanoma and orthotopic 4T1 breast tumor growth were remarkably restrained and pulmonary metastasis was prevented in immunocompetent mice. It is worth noting that this therapeutic effect partially resulted from the antitumor activity of neutrophils and lymphocytes due to inflammatory responses caused by bacterial infections. No toxicity was observed in the animal during the experiments. This study indicates thatE. coliNissle 1917 could be a potential carrier to deliver antitumor drugs effectively for cancer therapy.

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27

Lawton, S. A., and C. Anthony. "The role of blue copper proteins in the oxidation of methylamine by an obligate methylotroph." Biochemical Journal 228, no. 3 (June 15, 1985): 719–26. http://dx.doi.org/10.1042/bj2280719.

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Organism 4025, an obligate methylotroph, when grown on methylamine in the presence of a high concentration of copper, contained high concentrations of methylamine dehydrogenase and two blue copper proteins, amicyanin and an azurin-type protein; these were purified to homogeneity and characterized. The methylamine dehydrogenase is a basic protein (pI 8.8) and consists of light and heavy subunits (Mr 14100 and 43000; total Mr 112000). This dehydrogenase differed slightly from other methylamine dehydrogenases in its absorption spectrum and in its lack of thermal stability. Amicyanin, the more abundant blue copper protein, had an Mr of 11500, a midpoint redox potential of 294mV at pH 7.0, and a much lower isoelectric point (pI5.3) than other amicyanins. Its absorption maximum was 620 nm (7-24 nm higher than those of other amicyanins); its absorption coefficient (at 620 nm) was 3.8 mM-1 X cm-1. The ‘azurin’ (6% of the blue copper protein) had an Mr of 12500, a midpoint redox potential of 323 mV and a high isoelectric point (pI 9.4). Its absorption maximum was 620 nm, the absorption coefficient (16 mM-1 X cm-1) at this wavelength being considerably greater than that of any blue copper protein described previously. The partially-purified soluble cytochromes cH and cL were similar to those of other methylotrophs. The interactions of the purified redox proteins were investigated in order to elucidate their role in methylamine oxidation. Methylamine dehydrogenase was able to donate electrons only to amicyanin, the rate of reaction being 2.04 mmol/min per mumol of methylamine dehydrogenase; this is sufficient to account for the rate of respiration in whole bacteria. The blue copper proteins were able to react rapidly with each other and with both the soluble cytochromes c.

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28

Gao, Meng, Jingjing Zhou, Zhengding Su, and Yongqi Huang. "Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy." Protein Science 26, no. 12 (October 27, 2017): 2334–41. http://dx.doi.org/10.1002/pro.3310.

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29

Witharana, Chamindri, and RanmuniBhagya Lakshani Dharmawickreme. "Bacterial protein azurin and tumour suppressor p53 in cancer regression." Advances in Human Biology 11, no. 2 (2021): 147. http://dx.doi.org/10.4103/aihb.aihb_69_20.

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30

Webb, M. Adam, and Glen R. Loppnow. "Protein Tuning of Excited-State Charge-Transfer Dynamics in Azurin." Journal of Physical Chemistry B 102, no. 44 (October 1998): 8923–29. http://dx.doi.org/10.1021/jp982316n.

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31

Kofman, V., O. Farver, I. Pecht, and D. Goldfarb. "Two-Dimensional Pulsed EPR Spectroscopy of the Copper Protein Azurin." Journal of the American Chemical Society 118, no. 5 (January 1996): 1201–6. http://dx.doi.org/10.1021/ja952704s.

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32

Karlsson, B. Göran, Torbjörn Pascher, Margareta Nordling, Rolf H. A. Arvidsson, and Lennart G. Lundberg. "Expression of the blue copper protein azurin fromPseudomonas aeruginosainEscherichia coli." FEBS Letters 246, no. 1-2 (March 27, 1989): 211–17. http://dx.doi.org/10.1016/0014-5793(89)80285-6.

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33

Apiyo, David, and Pernilla Wittung-Stafshede. "Unique complex between bacterial azurin and tumor-suppressor protein p53." Biochemical and Biophysical Research Communications 332, no. 4 (July 2005): 965–68. http://dx.doi.org/10.1016/j.bbrc.2005.05.038.

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34

Choi, Jeong-Woo, Byung-Keun Oh, Young Jun Kim, and Junhong Min. "Protein-based biomemory device consisting of the cysteine-modified azurin." Applied Physics Letters 91, no. 26 (December 24, 2007): 263902. http://dx.doi.org/10.1063/1.2828046.

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35

Sato, M., H. Watanabe, and T. Kohzuma. "Studies on the crystal growth of blue copper protein azurin I and azurin II from Alcaligenes xylosoxidans NCIMB 11015." Seibutsu Butsuri 41, supplement (2001): S157. http://dx.doi.org/10.2142/biophys.41.s157_1.

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36

Fereiro, Jerry A., Xi Yu, Israel Pecht, Mordechai Sheves, Juan Carlos Cuevas, and David Cahen. "Tunneling explains efficient electron transport via protein junctions." Proceedings of the National Academy of Sciences 115, no. 20 (April 30, 2018): E4577—E4583. http://dx.doi.org/10.1073/pnas.1719867115.

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Metalloproteins, proteins containing a transition metal ion cofactor, are electron transfer agents that perform key functions in cells. Inspired by this fact, electron transport across these proteins has been widely studied in solid-state settings, triggering the interest in examining potential use of proteins as building blocks in bioelectronic devices. Here, we report results of low-temperature (10 K) electron transport measurements via monolayer junctions based on the blue copper protein azurin (Az), which strongly suggest quantum tunneling of electrons as the dominant charge transport mechanism. Specifically, we show that, weakening the protein–electrode coupling by introducing a spacer, one can switch the electron transport from off-resonant to resonant tunneling. This is a consequence of reducing the electrode’s perturbation of the Cu(II)-localized electronic state, a pattern that has not been observed before in protein-based junctions. Moreover, we identify vibronic features of the Cu(II) coordination sphere in transport characteristics that show directly the active role of the metal ion in resonance tunneling. Our results illustrate how quantum mechanical effects may dominate electron transport via protein-based junctions.

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37

Romero-Muñiz, Carlos, María Ortega, Jose Guilherme Vilhena, Rubén Pérez, Juan Carlos Cuevas, and Linda A. Zotti. "The Role of Metal Ions in the Electron Transport through Azurin-Based Junctions." Applied Sciences 11, no. 9 (April 21, 2021): 3732. http://dx.doi.org/10.3390/app11093732.

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We studied the coherent electron transport through metal–protein–metal junctions based on a blue copper azurin, in which the copper ion was replaced by three different metal ions (Co, Ni and Zn). Our results show that neither the protein structure nor the transmission at the Fermi level change significantly upon metal replacement. The discrepancy with previous experimental observations suggests that the transport mechanism taking place in these types of junctions is probably not fully coherent.

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38

Faham, Salem, Michael W. Day, William B. Connick, Brian R. Crane, Angel J. Di Bilio, William P. Schaefer, Douglas C. Rees, and Harry B. Gray. "Structures of ruthenium-modified Pseudomonas aeruginosa azurin and [Ru(2,2′-bipyridine)2(imidazole)2]SO4·10H2O." Acta Crystallographica Section D Biological Crystallography 55, no. 2 (February 1, 1999): 379–85. http://dx.doi.org/10.1107/s0907444998010464.

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The crystal structure of Ru(2,2′-bipyridine)2(imidazole)(His83)azurin (RuAz) has been determined to 2.3 Å resolution by X-ray crystallography. The spectroscopic and thermodynamic properties of both the native protein and [Ru(2,2′-bipyridine)2(imidazole)2]2+ are maintained in the modified protein. Dark-green RuAz crystals grown from PEG 4000, LiNO3, CuCl2 and Tris buffer are monoclinic, belong to the space group C2 and have cell parameters a = 100.6, b = 35.4, c = 74.7 Å and β = 106.5°. In addition, [Ru(2,2′-bipyridine)2(imidazole)2]SO4·10H2O was synthesized, crystallized and structurally characterized by X-ray crystallography. Red–brown crystals of this complex are monoclinic, space group P21/n, unit-cell parameters a = 13.230 (2), b = 18.197 (4), c = 16.126 (4) Å, β = 108.65 (2)°. Stereochemical parameters for the refinement of Ru(2,2′-bipyridine)2(imidazole)(His83) were taken from the atomic coordinates of [Ru(2,2′-bipyridine)2(imidazole)2]2+. The structure of RuAz confirms that His83 is the only site of chemical modification and that the native azurin structure is not perturbed significantly by the ruthenium label.

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39

YANG, D., X. MIAO, Z. YE, J. FENG, R. XU, X. HUANG, and F. GE. "Bacterial redox protein azurin induce apoptosis in human osteosarcoma U2OS cells." Pharmacological Research 52, no. 5 (November 2005): 413–21. http://dx.doi.org/10.1016/j.phrs.2005.06.002.

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40

Ainscough, Eric W., Alistair G. Bingham, Andrew M. Brodie, Walther R. Ellis, Harry B. Gray, Thomas M. Loehr, Jeffrey E. Plowman, Gillian E. Norris, and Edward N. Baker. "Spectrochemical studies on the blue copper protein azurin from Alcaligenes denitrificans." Biochemistry 26, no. 1 (January 13, 1987): 71–82. http://dx.doi.org/10.1021/bi00375a011.

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41

Wittung-Stafshede, Pernilla. "Role of Cofactors in Folding of the Blue-Copper Protein Azurin." Inorganic Chemistry 43, no. 25 (December 2004): 7926–33. http://dx.doi.org/10.1021/ic049398g.

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42

Delfino, Ines, and Salvatore Cannistraro. "Optical investigation of the electron transfer protein azurin–gold nanoparticle system." Biophysical Chemistry 139, no. 1 (January 2009): 1–7. http://dx.doi.org/10.1016/j.bpc.2008.09.016.

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43

Coremans, J. W. A., M. van Gastel, O. G. Poluektov, E. J. J. Groenen, T. den Blaauwen, G. van Pouderoyen, G. W. Canters, H. Nar, C. Hammann, and A. Messerschmidt. "An ENDOR and ESEEM study of the blue copper protein azurin." Chemical Physics Letters 235, no. 3-4 (March 1995): 202–10. http://dx.doi.org/10.1016/0009-2614(95)00114-j.

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44

Venkat, Anurag Setty, Stefano Corni, and Rosa Di Felice. "Electronic Coupling Between Azurin and Gold at Different Protein/Substrate Orientations." Small 3, no. 8 (August 3, 2007): 1431–37. http://dx.doi.org/10.1002/smll.200700001.

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45

Liu, Jing, Katlyn K. Meier, Shiliang Tian, Jun-long Zhang, Hongchao Guo, Charles E. Schulz, Howard Robinson, Mark J. Nilges, Eckard Münck, and Yi Lu. "Redesigning the Blue Copper Azurin into a Redox-Active Mononuclear Nonheme Iron Protein: Preparation and Study of Fe(II)-M121E Azurin." Journal of the American Chemical Society 136, no. 35 (August 22, 2014): 12337–44. http://dx.doi.org/10.1021/ja505410u.

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46

Sereena, M., and Denoj Sebastian. "Molecular Detection of Azurin: A Powerful Anticancer Protein from Native Pseudomonas Isolates." Journal of Advances in Medical and Pharmaceutical Sciences 5, no. 1 (January 10, 2016): 1–7. http://dx.doi.org/10.9734/jamps/2016/20557.

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47

Belhadj, Mahfoud, John M. Jean, Richard A. Friesner, John Schoonover, and William H. Woodruff. "Theoretical analysis of resonance Raman spectra from the blue copper protein azurin." Journal of Physical Chemistry 94, no. 5 (March 1990): 2160–66. http://dx.doi.org/10.1021/j100368a078.

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48

Friis, E. P., J. E. T. Andersen, L. L. Madsen, P. Møller, and J. Ulstrup. "In situ STM and AFM of the copper protein Pseudomonas aeruginosa azurin." Journal of Electroanalytical Chemistry 431, no. 1 (June 1997): 35–38. http://dx.doi.org/10.1016/s0022-0728(97)00178-2.

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49

Pompa, P. P., A. Bramanti, G. Maruccio, L. L. del Mercato, R. Cingolani, and R. Rinaldi. "Ageing of solid-state protein films: Behavior of azurin at ambient conditions." Chemical Physics Letters 404, no. 1-3 (March 2005): 59–62. http://dx.doi.org/10.1016/j.cplett.2005.01.076.

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Paydarnia, Nafiseh, Shahryar Khoshtinat Nikkhoi, Azita Fakhravar, Mohsen Mehdiabdol, Hedieh Heydarzadeh, and Saeed Ranjbar. "Synergistic effect of granzyme B-azurin fusion protein on breast cancer cells." Molecular Biology Reports 46, no. 3 (April 1, 2019): 3129–40. http://dx.doi.org/10.1007/s11033-019-04767-x.

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