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 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 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

The Action Potential in Chara corallina III.* The Hodgkin-Huxley Parameters for the Plasmalemma

1979 ◽  
Vol 6 (3) ◽  
pp. 337 ◽  
Author(s):  
M.J Beilby ◽  
H.G.L Coster
Keyword(s):  
Experimental Data ◽  
Action Potential ◽  
Ionic Currents ◽  
Chara Corallina ◽  
Wide Range ◽  
Time Courses ◽  
Model Equations ◽  
Excitation Processes ◽  
Ionic Components ◽  
Peak Value

An analysis, based on the Hodgkin-Huxley (H-H) equations is given of excitation processes in the plasmalemma of cells of C. corallina. Voltage clamp data for the plasmalemma show the presence of two activation and two inactivation processes and both of these transients are modelled in a manner analagous to the gated Na+ current in squid axons. Separation of the various ionic components of the experimental clamp currents was achieved by fitting the experimental data over a wide range of potentials to the model equations. The potential dependencies of the various H-H parameters for C. corallina, determined from the analysis of experimental results, are presented. A reconstruction is also given of the action potential and it is shown to be in satisfactory agreement with the experimental data. Comparisons are made of the experimental and predicted threshold potential, refractory period and the effects of the external Cl- and Ca�+ ion concentrations on the action potential. From the H-H parameters, the time courses during an action potential of the conductances g*Cl, g*x (� g*Ca?), the non activated/inactivated steady-state conductance g*ss, and the corresponding ionic currents I*Cl, I*x (� I*Ca?) and I*ss are calculated. While in the H-H analysis the peak value of g*x is found to be very large (larger than the peak value of g*Cl), it is shown that nevertheless I*Cl and I*ss dominate during an action potential.

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

Photolytic studies on cytochrome c peroxidase from Pseudomonas aeruginosa

1985 ◽  
Vol 13 (3) ◽  
pp. 625-626
Author(s):  
COLIN GREENWOOD ◽  
NICHOLAS FOOTE ◽  
JIM PETERSON ◽  
ANDREW THOMSON
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase

scholarly journals Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa

Structure ◽  
1995 ◽  
Vol 3 (11) ◽  
pp. 1225-1233 ◽  
Author(s):  
Vilmos Fülöp ◽  
Christopher J Ridout ◽  
Colin Greenwood ◽  
Jénos Hajdu
Keyword(s):  
Crystal Structure ◽  
Pseudomonas Aeruginosa ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase
Sign in / Sign up

Export Citation Format

Share Document