Kinetics of electron transfer between mitochondrial cytochrome c and iron hexacyanides.
Abstract: The reduction of horse and Candida krusei cytochromes c by ferrocyanide has been studied by 1H NMR spectroscopy and the reaction found to involve a precursor complex of ferrocyanide bound to ferricytochrome c (pH* 7.4, 2H2O, I = 0.12, and 25 degrees C). The electron transfer rate constants for the reduction of the two ferricytochromes by associated ferrocyanide were found to be the same at 780 +/- 80 sec-1 but the association constants for binding of ferrocyanide to ferricytochrome c were significantly different: horse, 90 +/- 20 M-1 and Candida, 285 +/- 30 M-1. The different association constants partly accounts for the previously observed reactivity difference between horse and Candida cytochromes c. Comparison of the NMR data with data obtained by other kinetic methods has allowed the electron transfer rate constant for the oxidation of ferrocytochrome c by associated ferricyanide to be determined. This was found to be 4.6 +/- 1 X 10(4) sec-1.
Publication Date: 1984-08-01 PubMed ID: 6090588DOI: 10.1016/0162-0134(84)85052-7Google Scholar: Lookup
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- Journal Article
Summary
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This research observes the reduction process of horse and Candida krusei cytochromes c by ferrocyanide using 1H NMR spectroscopy. The scientists discovered that electron transfer rate constants between the two are the same, but the binding association constants show a difference. This difference influences the varying reactivity between the horse and Candida cytochromes c.
Reduction of Cytochromes c by Ferrocyanide
- The study explores the reduction of two different types of cytochromes c – horse and Candida krusei – by ferrocyanide using 1H NMR spectroscopy.
- The researchers found that the reduction reaction involves a precursor complex of ferrocyanide bound to ferricytochrome c.
Electron Transfer Rate Constants & Association Constants
- Data showed that the electron transfer rate constants for the reduction of both the horse and Candida cytochromes c by associated ferrocyanide were the same, valued at 780 +/- 80 sec-1.
- Interestingly, the association constants for ferrocyanide binding to the ferricytochrome c were found to be different: 90 +/- 20 M-1 for horse and 285 +/- 30 M-1 for Candida. This indicates that the binding strength of ferrocyanide to cytochrome c is higher in the case of Candida than in horses.
Effect on Reactivity and Electron Transfer Rate for Ferrocytochrome c Oxidation
- The different association constants discerned contribute to the previously observed reactivity difference between the horse and Candida cytochromes c. This signifies that the efficiency or speed of reactions involving cytochrome c may differ depending on the species considered.
- The researchers compared the NMR data with data obtained by other kinetic methods to determine the electron transfer rate constant for the oxidation of ferrocytochrome c by associated ferricyanide. They found this value to be 4.6 +/- 1 X 10(4) sec-1.
Cite This Article
APA
Eley CG, Ragg E, Moore GR.
(1984).
Kinetics of electron transfer between mitochondrial cytochrome c and iron hexacyanides.
J Inorg Biochem, 21(4), 295-310.
https://doi.org/10.1016/0162-0134(84)85052-7 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Candida / metabolism
- Cytochrome c Group / metabolism
- Electron Transport
- Ferricyanides
- Horses
- Kinetics
- Mathematics
- Mitochondria / metabolism
Citations
This article has been cited 2 times.- Lai B, Bernhardt PV, Krömer JO. Cytochrome c Reductase is a Key Enzyme Involved in the Extracellular Electron Transfer Pathway towards Transition Metal Complexes in Pseudomonas Putida.. ChemSusChem 2020 Oct 7;13(19):5308-5317.
- Dixon DW, Hong X, Woehler SE. Electrostatic and steric control of electron self-exchange in cytochromes c, c551, and b5.. Biophys J 1989 Aug;56(2):339-51.
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