Backbone dynamics and hydrogen exchange of Pseudomonas aeruginosa ferricytochrome c 551

BS Russell, L Zhong, M Bigotti, F Cutruzzolà… - JBIC Journal of …, 2003 - Springer
A model-free analysis of Pseudomonas aeruginosa ferricytochrome c 551 dynamics based
on 15 NR 1, 15 NR 2, and {1 H}-15 N heteronuclear nuclear Overhauser effect data is …

Electrochemical study of the intermolecular electron transfer to Pseudomonas aeruginosa cytochrome cd1 nitrite reductase

E Lojou, F Cutruzzola, M Tegoni, P Bianco - Electrochimica acta, 2003 - Elsevier
The kinetics of electron transfer reaction between cytochrome cd1 nitrite reductase (NiR)
from Pseudomonas aeruginosa and various physiological/non physiological redox partners …

Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c551 from Pseudomonas aeruginosa

S Gianni, C Travaglini-Allocatelli, F Cutruzzolà… - Journal of Molecular …, 2001 - Elsevier
Cytochrome c551 (cyt c551) from Pseudomonas aeruginosa is a small protein (82 residues)
that folds via a three-state pathway with the accumulation in the microsecond time-range of a …

Stability and physicochemical properties of the bovine brain phosphatidylethanolamine‐binding protein

B Vallée, C Teyssier, R Maget‐Dana… - European journal of …, 1999 - Wiley Online Library
The equilibrium behaviour of the bovine phosphatidylethanolamine‐binding protein (PEBP)
has been studied under various conditions of pH, temperature and urea concentration. Far …

Dynamic effects of mutations within two loops of cytochrome c551 from Pseudomonas aeruginosa

MA Ceruso, A Grottesi, A Di Nola - Proteins: Structure, Function …, 2003 - Wiley Online Library
In this work, we investigated the structural and dynamic consequences of two substitutions,
P58A and G36P, located in two different solvent‐exposed loops of cytochrome c551. The …

Tuning the Reduction Potential of Engineered Cytochrome c-553

A Fantuzzi, S Sadeghi, F Valetti, GL Rossi… - Biochemistry, 2002 - ACS Publications
Cytochrome c-553 from Desulfovibrio vulgaris exhibits a highly exposed heme and an
unusually low reduction potential with respect to other c-type cytochromes. Solvent heme …

Folding mechanism of Pseudomonas aeruginosa cytochrome c551: role of electrostatic interactions on the hydrophobic collapse and transition state properties

C Travaglini-Allocatelli, F Cutruzzolà, MG Bigotti… - Journal of molecular …, 1999 - Elsevier
We report on the folding kinetics of the small 82 residue cytochrome c551 from
Pseudomonas aeruginosa. The presence of two Trp residues (Trp56 and Trp77) allows the …

Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551

LV Michel, KL Bren - JBIC Journal of Biological Inorganic Chemistry, 2008 - Springer
Hydrogen exchange rates for backbone amide protons of oxidized Pseudomonas
aeruginosa cytochrome c-551 (P. aeruginosa cytochrome c) have been measured in the …

Hydration analysis of Pseudomonas aeruginosa cytochrome c551 upon acid unfolding by dielectric relaxation spectroscopy

T Wazawa, T Miyazaki, Y Sambongi, M Suzuki - Biophysical chemistry, 2010 - Elsevier
Dielectric relaxation (DR) study was performed to reveal the hydration change of
Pseudomonas aeruginosa ferric cytochrome c551 (PA c551) in dilute aqueous solutions …

Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgaris

P Wittung-Stafshede - Protein science, 1999 - cambridge.org
To understand general aspects of stability and folding of c-type cytochromes, we have
studied the folding characteristics of cytochrome c553 from Desulfovibrio vulgaris …