Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase

Biochemistry ◽  
1974 ◽  
Vol 13 (1) ◽  
pp. 39-44 ◽  
Author(s):  
James E. Erman
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Equilibrium Studies ◽  
Cyanide Binding

scholarly journals Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase.

1978 ◽  
Vol 253 (10) ◽  
pp. 3730-3735
Author(s):  
T.L. Poulos ◽  
S.T. Freer ◽  
R.A. Alden ◽  
N.H. Xuong ◽  
S.L. Edwards ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Cyanide Binding

scholarly journals Apolar distal pocket mutants of yeast cytochrome c peroxidase: Hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants

2013 ◽  
Vol 1834 (1) ◽  
pp. 137-148 ◽  
Author(s):  
Anil K. Bidwai ◽  
Cassandra Meyen ◽  
Heather Kilheeney ◽  
Damian Wroblewski ◽  
Lidia B. Vitello ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Cyanide Binding

scholarly journals Thermodynamics of hydrogen cyanide and hydrogen fluoride binding to cytochrome c peroxidase and its Asn-82→Asp mutant

1994 ◽  
Vol 302 (2) ◽  
pp. 437-442 ◽  
Author(s):  
S F DeLauder ◽  
J M Mauro ◽  
T L Poulos ◽  
J C Williams ◽  
F P Schwarz
Keyword(s):  
Cytochrome C ◽  
Binding Constant ◽  
Binding Constants ◽  
Cytochrome C Peroxidase ◽  
Titration Calorimetry ◽  
Difference Spectroscopy ◽  
Cyanide Binding ◽  
Order Of Magnitude ◽  
Binding Enthalpy ◽  
Entropic Effects

The thermodynamics of binding of fluoride and cyanide to cytochrome c peroxidase (CCP) and its Asn-82-->Asp mutant (D82CCP) in phosphate and acetate buffer at an ionic strength of 0.15 mol.kg-1 from pH 5.0 to 7.1 were investigated by titration calorimetry at 289 and 297 K. The binding reactions are enthalpically driven. The fluoride-binding constants determined from the titration calorimetry results were in agreement with those determined from difference-spectroscopy measurements. For cyanide binding to CCP at 297.9 K, the binding constant decreased from 8.95 (+/- 0.83) x 10(5) M-1 at pH 7.0 to 4.04(+/- 0.23) x 10(5) M-1 at pH 5.0, and the binding enthalpy increased from -57.2 +/- 1.4 kJ.mol-1 at pH 7.0 to -48.6 +/- 1.8 kJ.mol-1 at pH 5.0. For fluoride binding to CCP, the binding constant increased from 8.41(+/- 0.54) x 10(3) M-1 at pH 7.0 to 3.11(+/- 0.09) x 10(5) M-1 at pH 5.0 and the binding enthalpy increased from -71.9 +/- 1.1 kJ.mol-1 at pH 7.0 to -67.0 +/- 1.9 kJ.mol-1 at pH 5.0. The binding enthalpies for D82CCP were about the same as those for CCP. However, the binding constants for cyanide and fluoride to D82CCP were respectively a factor of two less and at least an order of magnitude less than the corresponding binding constants of CCP. Decreased ligand-binding strength in the D82CCP mutant is thus entirely due to entropic effects.

Kinetics of cyanide binding by half-reduced Pseudomonas cytochrome c peroxidase

1985 ◽  
Vol 828 (1) ◽  
pp. 67-72 ◽  
Author(s):  
Marjaana Rönnberg ◽  
Anne-Marie Lambeir ◽  
Nils Ellfolk ◽  
H.Brian Dunford
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Cyanide Binding ◽  
Kinetics Of

scholarly journals Conversion of the proximal histidine ligand to glutamine restores activity to an inactive mutant of cytochrome c peroxidase.

1992 ◽  
Vol 267 (36) ◽  
pp. 25656-25659
Author(s):  
K Choudhury ◽  
M Sundaramoorthy ◽  
J.M. Mauro ◽  
T.L. Poulos
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase
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