Results 171 to 180 of about 6,022 (216)
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Photochemistry and Photobiology, 1992
Abstract— The tryptophan phosphorescence from a series of derivatives of Pseudomonas aeruginosa azurin has been monitored at 30°C in pH 8.5 buffer solution. The phosphorescence lifetimes fall in the range of 230–270 ms for deoxygenated solutions of derivatives containing Cd(II), Cu(I), Co(II), Ni(II), Hg(II) or apoazurin. A weak signal with a lifetime
F K, Klemens, D R, McMillin
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Abstract— The tryptophan phosphorescence from a series of derivatives of Pseudomonas aeruginosa azurin has been monitored at 30°C in pH 8.5 buffer solution. The phosphorescence lifetimes fall in the range of 230–270 ms for deoxygenated solutions of derivatives containing Cd(II), Cu(I), Co(II), Ni(II), Hg(II) or apoazurin. A weak signal with a lifetime
F K, Klemens, D R, McMillin
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CuA centers and their biosynthetic models in azurin
JBIC Journal of Biological Inorganic Chemistry, 2010Cu(A) is a binuclear copper center that functions as an electron transfer agent, cycling between a reduced Cu(I)Cu(I) state and an oxidized mixed-valence Cu(+1.5)...Cu(+1.5) state. The copper ions are bridged by two cysteine thiolate ligands and form a copper-copper bond, the first reported of its kind in Nature.
Masha G, Savelieff, Yi, Lu
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Chemical modification of methionine residues in azurin
Biochemical and Biophysical Research Communications, 1979Abstract Azurin from Pseudomonas aeruginosa has been treated with bromoacetate at low pH to alkylate methionine residues. Two classes of methionine side chains are observed as a result of these reactions — four of the six methionines are reactive at pH 4, whereas all six are reactive at pH 3.2. The product containing four alkylated methionines
R H, Marks, R D, Miller
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The Crystal Structure of Nickel(II)-Azurin
European Journal of Biochemistry, 1995The nickel(II)-azurin metalloderivative has been crystallized and its structure solved at 0.205-nm resolution by X-ray diffraction. The overall structure is not modified by the metal exchange and the only differences with regard to the native copper(II)-azurin occur in the metal site region. These variations affect principally the axial ligands. Nickel
J M, Moratal +4 more
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The origin of the intense absorption in azurin
Bioinorganic Chemistry, 1978The intense visible absorption band of native azurin and the corresponding transitions of the Ni(II) and the Co(II) derivatives were analyzed. The bands were shown to be analogous ligand-to-metal charge transfer transitions and the optical electronegativity of the ligand involved is estimated to be 2.6.
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Purification and properties of Paracoccus denitrificans azurin
Archives of Biochemistry and Biophysics, 1980Abstract The isolation of an azurin type Cu protein from Paracoccus denitrificans (ATCC 13543) is described and some properties are reported. The purified protein has a molecular weight of 13,790 in a single polypeptide chain and contains one Cu atom per molecule.
K, Martinkus +3 more
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The reaction of Pseudomonas azurin with hydrated electrons
Biochemical and Biophysical Research Communications, 1971Abstract The reaction of azurin, the bacterial “blue” copper protein, with hydrated electrons has been investigated by the pulse radiolysis technique. The single Cu(II) ion of this protein was found to be reduced in a direct bimolecular reaction with the hydrated electron at a specific rate of 1.0 ± 0.3 × 10 11 M −1 sec −1 .
M, Faraggi, I, Pecht
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Optical and magnetic properties of pseudomonas azurins
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968Abstract 1. 1.The visible absorption spectra and optical rotatory dispersion spectra have been recorded for the azurins from Pseudomonas aeruginosa and Pseudomonas fluorescens. The magnitude of the Cotton effects in the visible range is indicative of a large degree of asymmetry of the copper-binding site. 2.
A S, Brill, G F, Bryce, H J, Maria
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The fine structure of luminescence spectra of azurin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1977The spectra of azurin absorption, fluorescence, phosphorescence and fluorescence excitation have been measured in aqueous solutions at ordinary and liquid nitrogen temperatures. The fluorescence spectra of azurin even at ordinary temperatures have a well resolved fine vibrational structure.
E A, Burstein +4 more
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Solvent Isotope Effects on Azurin Thermal Unfolding
The Journal of Physical Chemistry B, 1998The thermal unfolding of azurin in D2O has been investigated by differential scanning calorimetry, optical density measurements, and electron paramagnetic resonance spectroscopy, The study has allowed us to relate the local conformational changes occurring around the active site of azurin with the unfolding of the whole protein as the temperature ...
GUZZI, Rita +4 more
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