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Showing 1 to 20 of 24 for “"azurin"”.
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Probing the roles of metal binding ligands in cupredoxins: incorporating nonproteinogenic amino acids into azurin and CuA Azurin
Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2010-05-13T19:03:20Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 1 Clark_Kevin.pdf: 14900477 bytes, checksum: 901cc6f1c2f90be4a62e58094e6f0b6d (MD5)
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Probing the Roles of Metal Binding Ligands in Cupredoxins: Incorporating Nonproteinogenic Amino Acids Into Azurin and Copper a Azurin
… function of individual metal ligand residues in azurin and CuA azurin by using EPL to incorporate nonproteinogenic amino acid analogues has been demonstrated. This work has resulted in new insights into the role of the metal ligands and has shaped future metalloprotein engineering efforts.
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Toward Engineering Oxygenase Activity into the Electron Transfer Protein Azurin
… approach to small molecule processing in the azurin scaffold is demonstrated through description of the first reported Cu(II)-sulfenic acid species. This species, prepared in high yield through copper mediated reduction of hydrogen peroxide, represents the first reported chemical …
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Fluorescence Depolarization Study of Internal Tryptophan Mobility in Hydrated Azurin Films
… steady state fluorescence depolarization on azurin, which has a single tryptophan residue well-buried in the hydrophobic interior. Azurin was imbedded in a thin, solid, water-permeable polymer film. This procedure inhibited whole-protein motion while allowing examination of internal degrees …
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Fluorenscence depolarization study of internal tryptophan mobility in hydrated azurin films
… steady state fluorescence depolarization on azurin, which has a single tryptophan residue well-buried in the hydrophobic interior. Azurin was imbedded in a thin, solid, water-permeable polymer film. This procedure inhibited whole-protein motion while allowing examination of internal degrees …
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Metalloprotein engineering with unnatural amino acids: application in functional heme-copper oxidase and azurin
… and significantly improve O2 consumption rate. Azurin is a Type 1 copper protein involved in biological electron transfer. The copper ion in azurin is coordinated by two histidines and one cysteine in equatorial position and methionine, backbone oxygen of glycine at axial position. The …
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Designing Novel Blue Copper and Purple CuA Centers in Azurin With Natural and Unnatural Amino Acids
… binding loop from human ferrochelatase into azurin. Preliminary iron binding studies indicate the assembly of a 4Fe-4S or a 2Fe-2S iron sulfur cluster.
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Measured Electron Spin Relaxation Rates in Frozen Solutions of Azurin, Vitamin-B12r, and Nitrosyl Ferrous Myoglobin
… K are reported for a copper-containing protein, azurin, and a cobalt-containing biomolecular complex, vitamin B$\sb{\rm 12r}$, the paramagnetic product of the photolysis of coenzyme B$\sb $. Results are interpreted in terms of a spectral dimensionality. Rates are also reported for nitrosyl …
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Measured electron spin relaxation rates in frozen solutions of azurin: Vitamin B12r and nitrosyl ferrous myoglobin
… K are reported for a copper-containing protein, azurin, and a cobalt -containing bi omol ecul ar complex, vitamin B 12r, which is the paramagnetic product of the photolysis of coenzyme B 12. The results are interpreted in terms of a spectral dimensianality. Rates are also reported for nitrosyl …
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Protein engineering using azurin as the scaffold: capturing and studying novel metal-sulfenate and metal-NO species
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2018-05-01
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Engineering a Purple copper(A) Site Into the Blue Copper Protein Azurin: Construction, Spectroscopy, and Metal Substitution Studies
Metal substitution studies of azurin-CuA have been performed using various metal ions (i.e., Hg2+, Ag+, Cu +, Cd+, Rh2+, Au+, Co 2+, and Ni2+). Metal binding was determined by electronic absorption and electrospray mass spectrometry. The results obtained from theses studies indicate that there are …
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Modulation of Metal Coordination and Redox Properties of the Engineered Purple copper(A) and Ferrocene Centers in Azurin
Finally, the temperature effect on the pH of biological buffers was studied. Colorimetric determination of apparent pH using indicator dyes revealed significant changes in the apparent pH of buffer solutions at cryotemperatures.
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Isolating, characterizing, and engineering novel Cu-proteins and peroxidases
… work is on tuning the reduction potential of azurin, a common electron transfer protein. In chapter 3 I demonstrate that how by making mutations around the Cu site, and replacing Cu with Ni I can obtain an azurin variant with a reduction potential of nearly 1V, the highest potential that can …
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Structure/function relationships of the copper proteins nitrite reductase and rusticyanin
… formation with the physiological redox partners, azurin I and azurin II. This Trp residue was mutated to a His and its structure determined to 1.60 A. The ability of the Trp138His mutant to reduce nitrite was investigated using both an artificial donor and a physiological partner, azurin I. These …
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Expanding the chemistry of a cupredoxin by designing nonnative active sites and using abiological metals
… a mutant of the blue copper protein azurin (Az) was metalated with chromium and its novel properties were studied. Kinetic studies were performed on electron transfer reactions between Cr-Az, Cu-Az, and metal complexes such as hexaaquachromium(II) chloride and potassium ferricyanide. …
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Electron spin-lattice relaxation in two heme iron and two blue-copper proteins at liquid helium temperatures
… azide, bovine ferri-hemoglobin azide, cupric azurin (P. aeruginosa) and cupric spinach plastocyanin were measured at 9.5 GHz using the pulse-saturation recovery method. Measurements covered a temperature range of 1.4 K to as high as 22 K, with corresponding relaxation rates up to 10$\sp5$/sec. …
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Engineering heme-copper and multi-copper oxidases for efficient oxygen reduction catalysis
… in tuning reduction potentials of T1 Cu protein azurin, we have made significant progress in tuning the T1 Cu center in SLAC to decrease its over-potentials. We achieved the goal by structural overlays of the T1 Cu domain of SLAC and the high potential azurin reported by Lu group to search for …
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Electron spin-lattice relaxation in proteins, model heme complexes and ferricyanide solutions at helium temperatures
… for frozen solutions of the blue-copper proteins azurin and plastocyanin, the low-spin iron heme protein cytochrome-c, two (bis)imidazole ferric heme complexes in three different organic solvents and two ferricyanide solutions. Measurements were performed at X-band frequencies and temperatures …
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Outlier treatments using interolation on Malaysia tourist arrival forecasting: SARIMA and ANN approaches
Outliers are unusual observations that appear in a piece of data that are very different from the rest of the data. The presence of an outlier may directly affect the variance, the model parameters, and the overall estimation, especially during forecasting. To obtain an accurate forecast, any …
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The electron transport chains of Neisseria meningitidis
… a lesser extents than c4 or c2. Lipid-modified azurin (Laz) was heterologously expressed and purified. The purified protein contains copper ion and can be oxidized or reduced. When oxidized, Laz exhibits an intense blue colour and absorbs visible light around 626 nm. Laz can be oxidized by …
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