scholarly journals Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics

1983 ◽  
Vol 209 (3) ◽  
pp. 701-707 ◽  
Author(s):  
N Foote ◽  
A C Thompson ◽  
D Barber ◽  
C Greenwood
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cytochrome C ◽  
Isoelectric Focusing ◽  
Flash Photolysis ◽  
Cytochrome C Peroxidase ◽  
Acid Precipitation ◽  
Binding Kinetics ◽  
Stopped Flow ◽  
Purification Procedure ◽  
Kinetics Of

A procedure is described for the purification of cytochrome c peroxidase from Pseudomonas aeruginosa involving extraction by sonication, followed by acid precipitation and chromatography on only two types of gel. The final preparation had a purity ratio A407/A280 of 4.2, and was found to be essentially pure by isoelectric focusing. The enzyme was shown to be unstable during degassing under vacuum except in the presence of detergent. The kinetics of CO binding to dithionite-reduced peroxidase were studied with stopped-flow and flash-photolysis techniques, and the results obtained between pH 5 and 7 suggest the existence of two forms of dithionite-reduced enzyme in slow equilibrium.

scholarly journals A quantitative model for the mechanism of action of the cytochrome c peroxidase of Pseudomonas aeruginosa

1992 ◽  
Vol 283 (3) ◽  
pp. 839-843 ◽  
Author(s):  
N Foote ◽  
R Turner ◽  
T Brittain ◽  
C Greenwood
Keyword(s):  
Experimental Data ◽  
Pseudomonas Aeruginosa ◽  
Cytochrome C ◽  
Close Agreement ◽  
Cytochrome C Peroxidase ◽  
Quantitative Model ◽  
Activation Process ◽  
Stopped Flow ◽  
Wide Range ◽  
Time Courses

Each of the elementary reaction steps in both the activation process and catalytic cycle of the cytochrome c peroxidase of Pseudomonas aeruginosa was characterized using stopped-flow methods. A synthesis of these data led to the establishment of a quantitative model for the action of this enzyme. Comparisons were made between experimental data and calculations over a wide range of enzyme, reductant and H2O2 concentrations. Close agreement was found between empirical and simulated reaction time courses from millisecond to tens of seconds time ranges, giving us confidence in the validity of the quantitative model of this enzyme's actions.

scholarly journals A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase

FEBS Letters ◽  
1995 ◽  
Vol 377 (2) ◽  
pp. 145-149 ◽  
Author(s):  
Bart Samyn ◽  
Kathleen Van Craenenbroeck ◽  
Lina De Smet ◽  
Isabel Vandenberghe ◽  
Graham Pettigrew ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Covalent Structure

Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: A mutagenesis studies

2007 ◽  
Vol 101 (8) ◽  
pp. 1133-1139 ◽  
Author(s):  
Hsi-Chen Hsiao ◽  
Svetlana Boycheva ◽  
Nicholas J. Watmough ◽  
Thomas Brittain
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase

scholarly journals Kinetics of CO Ligation with Nitric-oxide Synthase by Flash Photolysis and Stopped-flow Spectrophotometry

1997 ◽  
Vol 272 (19) ◽  
pp. 12523-12528 ◽  
Author(s):  
Jürgen S. Scheele ◽  
Vladimir G. Kharitonov ◽  
Pavel Martásek ◽  
Linda J. Roman ◽  
Vijay S. Sharma ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Flash Photolysis ◽  
Stopped Flow ◽  
Oxide Synthase ◽  
Kinetics Of

A rapid-scan spectrometric and stopped-flow study of Compound I and Compound II of Pseudomonas cytochrome c peroxidase

1985 ◽  
Vol 236 (2) ◽  
pp. 714-719 ◽  
Author(s):  
Marjaana Rönnberg ◽  
Anne-Marie Lambeir ◽  
Nils Ellfolk ◽  
H.Brian Dunford
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Stopped Flow ◽  
Compound I ◽  
Rapid Scan ◽  
Compound Ii ◽  
Flow Study
Sign in / Sign up

Export Citation Format

Share Document