Results 181 to 190 of about 6,022 (216)

Water Effects on Electron Transfer in Azurin Dimers

The Journal of Physical Chemistry B, 2006
Recent experimental and theoretical analyses indicate that water molecules between or near redox partners can significantly affect their electron-transfer (ET) properties. Here, we study the effects of intervening water molecules on the electron self-exchange reaction of azurin (Az) by using a newly developed ab-initio method to calculate transfer ...
Migliore A, Corni S, Di Felice R, Molinari E   +3 more
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A crystallographic model for azurin at 3 Å resolution

Journal of Molecular Biology, 1978
Abstract The structure of the blue copper protein azurin (Mr 14,000) from Pseudomonas aeruginosa has been determined from a 3.0 A resolution electron density map computed with phases based on a uranyl derivative to 3 A resolution and a platinum derivative to 3.7 A. Interpretation of the somewhat noisy map was based on comparison of the density of the
E T, Adman, R E, Stenkamp, L C, Sieker, L H, Jensen   +3 more
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Folding degrees of azurins and pseudoazurins

Computational Biology and Chemistry, 2005
A quantitative measure of the degree of folding of azurins and pseudoazurins has been made. We have found that the reduction potential of azurins and pseudoazurins is a function of the contribution to the degree of folding of His117, a key amino acid in electron transfer which is directly bonded to copper in these proteins. The folding degree of His117
Ernesto Estrada, Eugenio Uriarte
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Electron Transfer in Homologous Azurins

Topical Meeting on Ultrafast Phenomena, 1986
Using time correlated single photon counting, we have studied electron transfer rates, kET in the homologous blue-copper proteins, azurins, obtained from Pseudomonas aeruginosa (Pae) and Alcaligenes faecalis (Afe). The salient difference between these proteins lies in the position of their single tryptophan residues.
J.W. Petrich, J.W. Longworth, G.R. Fleming   +2 more
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Studies of thermally induced denaturation of azurin and azurin derivatives by differential scanning calorimetry: evidence for copper selectivity

Biochemistry, 1986
Azurin, a blue copper protein from Pseudomonas aeruginosa, and several derivatives of azurin have been studied by differential scanning calorimetry. Two well-separated, irreversible transitions are observed in a scan of apoazurin under a variety of conditions, and they are assigned to distinct steps in the denaturation process.
H R, Engeseth, D R, McMillin
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Specific Anions Effects of on the Stability of Azurin in Ice

The Journal of Physical Chemistry B, 2008
This investigation represents a first attempt to gain a quantitative estimate of the effects of the anions sulfate, citrate, acetate, chloride and thiocyanate on the thermodynamic stability (DeltaG degrees) of a model globular protein in ice at -15 degrees C.
Strambini GB, Gonnelli M
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Effects of Sugars and Polyols on the Stability of Azurin in Ice

The Journal of Physical Chemistry B, 2008
This study represents the first attempt to gain a quantitative estimate of the protective influence of sugars (sucrose and trehalose) and polyols (sorbitol and glycerol) on the thermodynamic stability (DeltaG degrees ) of a protein in low-temperature part-frozen aqueous solutions.
Strambini GB, Balestreri E, Galli A, Gonnelli M   +3 more
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Redox properties of an engineered purple CuA azurin

Archives of Biochemistry and Biophysics, 2002
Purple Cu(A) centers are a class of binuclear, mixed-valence copper complexes found in cytochrome c oxidase and nitrous oxide reductase. An engineered Cu(A) protein was formed by replacing a portion of the amino acid sequence that contains three of the ligands to the native type I copper center of Pseudomonas aeruginosa azurin with the corresponding ...
Dapeng, Sun, Xiaotang, Wang, Victor L, Davidson   +2 more
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Azurins and Their Site-Directed Mutants

2002
The detailed knowledge of azurin structure and the new possibil-ities offered by site-directed mutagenesis make it a convenient model for studies on the stability of small globular proteins. In particular the importance of a very stable hydrophobic core for maintaining the native, biologically active conformation appears evident.
Giampiero Mei, Nicola Rosato, Alessandro Finazzi Agro   +2 more
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The kinetics of the cytochrome-c-azurin redox equilibrium

Biochemical and Biophysical Research Communications, 1973
Abstract A preliminary analysis of the temperature-jump relaxation spectrum of the cytochrome-c-azurin redox system from Pseudomonas fluorescens revealed two chemical relaxation times. These are explained in terms of two association steps and an electron transfer between the associated species.
I, Pecht, P, Rosen
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