Kinetic parameters for cytochrome c via insulated electrode voltammetry

Journal of the American Chemical Society

Volumn 118, Issue 33, 1996, Pages 7857-7858

  Terrettaz, Samuel ^a   Cheng, Jun ^a   Miller, Cary J ^a   Guiles, R D ^b  

^a UNIVERSITY OF MARYLAND   (United States)

^b UNIVERSITY OF MARYLAND   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C;

ANIMAL TISSUE; ARTICLE; CYCLIC POTENTIOMETRY; ENZYME KINETICS; FISH; HORSE; NONHUMAN; YEAST;

EID: 0029794492     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja960866y     Document Type: Article

References (25)

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22. -8 cm and a reorganization energy of 0.35 eV for the bound cytochrome and 0.61 eV for the solution species. The heterogeneous electron transfer rate constant is divided by the reaction layer thickness and corrected for the difference in the activation energies to obtain the corrected first-order rate estimate. See the supporting information for a more detailed explanation of this comparison.
23. This assumption of minimal interactions between the hydroxylated monolayer and the solution cytochrome is supported by the absence of any measurable preconcentration of the cytochrome at the interface as determined from chronocoulometric studies and the independence of the kinetic properties with the solution concentration of the cytochrome. Previous studies strongly suggest that there are minimal interactions between these hydroxlated surfaces and a range of redox molecules.
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