Results 11 to 20 of about 6,022 (216)

The Azurin Coding Gene: Origin and Phylogenetic Distribution [PDF]

open access: yesMicroorganisms, 2021
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.
Leandro Gammuto   +4 more
doaj   +9 more sources

Utilization of Cheese Whey for Production of Azurin by Pseudomonas aeruginosa

open access: yesSakarya Üniversitesi Fen Bilimleri Enstitüsü Dergisi, 2021
Azurin which has attracted much attention as potential anticancer agent in recent years is a bacterial secondary metabolite. This copper-containing redox protein secreted by Pseudomonas aeruginosa has capability of preferentially entering into many human
Yağmur Ünver
doaj   +2 more sources

Structural basis of bacterial effector protein azurin targeting tumor suppressor p53 and inhibiting its ubiquitination

open access: yesCommunications Biology, 2023
Structural and mutagenic analyses reveal the mechanistic basis of azurin-mediated p53 stabilization and tumor suppression, and several affinity-enhancing azurin mutants are designed.
Jianjian Hu   +9 more
doaj   +2 more sources

Photogeneration and Quenching of Tryptophan Radical in Azurin [PDF]

open access: yesThe Journal of Physical Chemistry B, 2015
Tryptophan and tyrosine can form radical intermediates that enable long-range, multistep electron transfer (ET) reactions in proteins. This report describes the mechanisms of formation and quenching of a neutral tryptophan radical in azurin, a blue-copper protein that contains native tyrosine (Y108 and Y72) and tryptophan (W48) residues.
Bethany C, Larson   +6 more
openaire   +3 more sources

Transient Absorption Spectroscopy of Blue Copper Sites in Divergent Protein Folds: Azurin Versus Multicopper Oxidase. [PDF]

open access: yesChemphyschem
Ultrafast pump‐probe spectroscopy of two evolutionarily divergent blue copper proteins reveals distinct low‐frequency ground‐state collective modes (38 cm−1 in SLAC, 29 cm−1 in azurin) generated via impulsive stimulated Raman scattering, potentially reflecting the differences in the rigidity of the surrounding protein scaffold beyond a conserved Cu ...
Domenianni LI, Kielb P.
europepmc   +2 more sources

Preliminary Analysis of the Presence of Bacterial Azurin Coding Gene in CRC Patients and Correlation with the Microbiota Composition

open access: yesFrontiers in Bioscience-Landmark, 2022
Background: Azurin, a bacterial cupredoxin firstly isolated from the bacterium Pseudomonas aeruginosa, is considered a potential alternative therapeutic tool against different types of cancer. Aims: In this work we have explored the relationship possibly
Marta Iozzo   +6 more
doaj   +1 more source

Efficient Electron Hopping Transport through Azurin-Based Junctions. [PDF]

open access: yesJ Phys Chem Lett, 2023
We conducted a theoretical study into electron transport through junctions of the blue-copper azurin from Pseudomonas aeruginosa. We found that single-site hopping can lead to either higher or lower current values compared to fully-coherent transport ...
Roldán-Piñero C   +6 more
europepmc   +2 more sources

Luminescence Quenching in Azurin [PDF]

open access: yesEuropean Journal of Biochemistry, 1973
The luminescence of oxidized or reduced azurin, an intensely blue copper protein, has been observed. The addition of Cu2+ or Hg2+ reduced the luminescence of the apoprotein to one third of its value while Ag+ reduced it to two thirds. This quenching is explained in terms of tryptophan distorsion produced by the different coordination of these metal ...
A, Finazzi-Agrò   +4 more
openaire   +2 more sources

A Proton ENDOR Study of Azurin [PDF]

open access: yesApplied Magnetic Resonance, 2009
As part of our ongoing project that aims at the optimum characterization of the electronic structure of the blue-copper site of azurin from Pseudomonas aeruginosa, we present the complete hyperfine tensors of the protons bound to the Cbeta atom of the copper-bound cysteine 112.
Sottini, S.   +6 more
openaire   +3 more sources

Sequence-specific destabilization of azurin by tetramethylguanidinium-dipeptide ionic liquids

open access: yesBiochemistry and Biophysics Reports, 2022
The thermal unfolding of the copper redox protein azurin was studied in the presence of four different dipeptide-based ionic liquids (ILs) utilizing tetramethylguanidinium as the cation.
Roshani Patel   +9 more
doaj   +1 more source

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