Axial ligation and heme environment in cytochrome c-555 from Prosthecochloris aestuarii. Investigation by absorption and solvent perturbation difference spectroscopy

Biochemistry ◽  
1978 ◽  
Vol 17 (6) ◽  
pp. 1028-1031 ◽  
Author(s):  
Michael D. Fiechtner ◽  
Richard J. Kassner
Keyword(s):  
Cytochrome C ◽  
Difference Spectroscopy ◽  
Axial Ligation ◽  
Prosthecochloris Aestuarii

scholarly journals Raman difference spectroscopy of heme-linked ionizations in cytochrome c peroxidase.

1983 ◽  
Vol 258 (4) ◽  
pp. 2168-2173
Author(s):  
J A Shelnutt ◽  
J D Satterlee ◽  
J E Erman
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Difference Spectroscopy

scholarly journals Protein influence on the heme in cytochrome c: evidence from Raman difference spectroscopy.

1979 ◽  
Vol 76 (8) ◽  
pp. 3865-3869 ◽  
Author(s):  
J. A. Shelnutt ◽  
D. L. Rousseau ◽  
J. K. Dethmers ◽  
E. Margoliashi
Keyword(s):  
Cytochrome C ◽  
Difference Spectroscopy

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.

Cytochrome c and SDS: A Molten Globule Protein with Altered Axial Ligation

2004 ◽  
Vol 336 (2) ◽  
pp. 489-496 ◽  
Author(s):  
Ivano Bertini ◽  
Paola Turano ◽  
Paul R. Vasos ◽  
Arnaud Bondon ◽  
Soizic Chevance ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Molten Globule ◽  
Axial Ligation

scholarly journals ATR-FTIR difference spectroscopy of the PM intermediate of bovine cytochrome c oxidase

2002 ◽  
Vol 1555 (1-3) ◽  
pp. 116-121 ◽  
Author(s):  
Masayo Iwaki ◽  
Jacques Breton ◽  
Peter R Rich
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Difference Spectroscopy ◽  
Ftir Difference Spectroscopy

scholarly journals The location of the polyphosphate-binding sites on cytochrome c measured by NMR paramagnetic difference spectroscopy

1991 ◽  
Vol 199 (3) ◽  
pp. 569-574 ◽  
Author(s):  
David W. CONCAR ◽  
David WHITFORD ◽  
R. J. P. WILLIAMS
Keyword(s):  
Cytochrome C ◽  
Binding Sites ◽  
Difference Spectroscopy
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