Kinetics of carbon monoxide binding to cytochrome c peroxidase: pH and carbon monoxide concentration effects

1984 ◽  
Vol 106 (21) ◽  
pp. 6448-6449
Author(s):  
Ann M. English ◽  
George McLendon ◽  
Karen Taylor
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Concentration Effects ◽  
Carbon Monoxide Concentration ◽  
Carbon Monoxide Binding ◽  
Kinetics Of

Carbon monoxide recombination in cytochrome c peroxidase: effect of the local heme environment on carbon monoxide binding explored through site-directed mutagenesis

Biochemistry ◽  
1990 ◽  
Vol 29 (7) ◽  
pp. 1777-1791 ◽  
Author(s):  
Mark A. Miller ◽  
Massimo Coletta ◽  
J. Matthew Mauro ◽  
Leslie D. Putnam ◽  
Martin F. Farnum ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Carbon Monoxide Binding

Carbon monoxide dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences carbon monoxide dissociation rates

Biochemistry ◽  
1990 ◽  
Vol 29 (42) ◽  
pp. 9978-9988 ◽  
Author(s):  
Mark A. Miller ◽  
J. Matthew Mauro ◽  
Giulietta Smulevich ◽  
Massimo Coletta ◽  
Joseph Kraut ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers

1974 ◽  
Vol 141 (1) ◽  
pp. 299-304 ◽  
Author(s):  
Silvestro Dupré ◽  
Maurizio Brunori ◽  
Michael T. Wilson ◽  
Colin Greenwood
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Unique Type ◽  
Horse Heart Cytochrome ◽  
Methionine Residue ◽  
Titration Data ◽  
Carbon Monoxide Binding ◽  
Horse Heart Cytochrome C ◽  
Kinetics Of ◽  
Recombination Kinetics

Studies on horse heart cytochrome c polymers were carried out by stopped-flow and photolysis techniques, to investigate the properties of the CO complex and the kinetics of electron transfer, mainly of the dimeric and tetrameric forms. CO binding, which does not occur with native monomers, proceeds at both pH7.0 and pH9.6, and appears to follow complex kinetics: an initial phase is observed, which is CO-concentration-dependent, followed by a very slow monomolecular phase (k~2×10-3s-1 at pH7) before establishment of equilibrium. Photodissociation of the CO complex has a very low quantum yield, probably less than 0.1. Static titration data of the dimer gave an ‘n’ value of 0.4. These data strongly suggest heterogeneity of the population of binding sites, and have been interpreted in terms of the existence of different structures, probably owing to the non-unique type of binding of monomers during polymerization. Polymers of cytochrome c carboxymethylated on the methionine residue normally ligated to iron show simple CO recombination kinetics after photolytic removal (kon=1.5×106m-1·s-1 at pH6). We therefore suggest that, for native cytochrome c, polymerization has an effect on the lability of the haem crevice, rendering the iron available for binding ligands, without, however, forming the structure of a truly open crevice. Electron transfer is, on the other hand, a simple process, and no gross differences are observed between monomer and polymers. A simple model, taking into account all these data, is suggested.

Thermodynamics of carbon monoxide binding to monomeric cytochrome c'

Biochemistry ◽  
1987 ◽  
Vol 26 (25) ◽  
pp. 8055-8058 ◽  
Author(s):  
Michael L. Doyle ◽  
Stanley J. Gill ◽  
Terrence E. Meyer ◽  
Michael A. Cusanovich
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Carbon Monoxide Binding
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