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Cytochrome c: ion binding and redox properties. Studies on ferri and ferro forms of horse, bovine, and tuna cytochrome c.
Abstract: The ion binding properties of horse, bovine, and tuna cytochrome c (both oxidized and reduced) have been measured using a combination of ultrafiltration, neutron activation, and ion chromatography. The ions investigated were chloride, phosphate, and Tris-cacodylate. Ion chromatography and neutron activation analysis techniques were employed to determine the concentration of free anions. Binding constants are obtained from modified Scatchard plots (in the range of 10-2000 M-1). The redox potentials for cytochrome c at different ionic strengths, pH 7.0, have been determined. In this paper we report the ionic strength and ion binding effects on the redox properties of horse, bovine, and tuna cytochrome c. Potential versus ionic strength dependence for horse, bovine, and tuna cytochrome c from the experimental data were compared with a theoretical model.
Publication Date: 1988-08-25 PubMed ID: 2841331 The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Comparative Study
- Journal Article
- Research Support
- U.S. Gov't
- Non-P.H.S.
Summary
This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.
This research paper explores the ion binding properties and redox potentials of horse, bovine, and tuna cytochrome c. Using several analytical techniques, the study investigates how ionic strength and different ions, like chloride, phosphate, and Tris-cacodylate, impact the redox properties of these cytochrome c samples.
Experimental Approach
- The researchers used three types of cytochrome c – from horse, bovine, and tuna – in both their oxidized (ferri) and reduced (ferro) forms, to study how each version interacts with certain ions.
- The ions being investigated were chloride, phosphate, and Tris-cacodylate.
- A combination of ultrafiltration, ion chromatography, and neutron activation analytical techniques were employed to measure ion binding properties of the cytochrome c samples.
- Ion chromatography and neutron activation analysis were specifically used to identify the concentration of free anions within the samples.
Data Interpretation and Results
- Binding constants were calculated using modified Scatchard plots, giving a range of 10-2000 M-1.
- The researchers also determined the redox potentials for each type of cytochrome c, at various ionic strengths, at a pH of 7.0, to understand how these conditions influenced redox properties.
- The study’s findings discuss how ionic strength and ion binding can affect the redox characteristics of the cytochrome c samples.
Comparison with Theoretical Models
- Their experimental data on potential versus ionic strength dependence for the three types of cytochrome c were cross-checked with a theoretical model.
- This comparison likely provided deeper insight into the behavior and properties of cytochrome c under different conditions and affirmed the research’s credibility and accuracy.
As a result, this research contributes to the broader understanding of cytochrome c – a protein crucial for cellular respiration – by elucidating its ion binding properties and how these, along with variations in ionic strength, affect its redox behavior.
Cite This Article
APA
Gopal D, Wilson GS, Earl RA, Cusanovich MA.
(1988).
Cytochrome c: ion binding and redox properties. Studies on ferri and ferro forms of horse, bovine, and tuna cytochrome c.
J Biol Chem, 263(24), 11652-11656.
Publication
Researcher Affiliations
- Department of Chemistry, University of Arizona, Tucson 85721.
MeSH Terms
- Animals
- Anions
- Cacodylic Acid / metabolism
- Cattle
- Chlorides / metabolism
- Chromatography
- Cytochrome c Group / metabolism
- Horses / metabolism
- Kinetics
- Neutron Activation Analysis
- Osmolar Concentration
- Oxidation-Reduction
- Phosphates / metabolism
- Tromethamine / metabolism
- Tuna / metabolism
Citations
This article has been cited 13 times.- Sławski J, Białek R, Burdziński G, Gibasiewicz K, Worch R, Grzyb J. Competition between Photoinduced Electron Transfer and Resonance Energy Transfer in an Example of Substituted Cytochrome c-Quantum Dot Systems. J Phys Chem B 2021 Apr 8;125(13):3307-3320.
- Secondo LE, Avrutin V, Ozgur U, Topsakal E, Lewinski NA. Real-time monitoring of cellular oxidative stress during aerosol sampling: a proof of concept study. Drug Chem Toxicol 2022 Mar;45(2):767-774.
- Deng Y, Zhong F, Alden SL, Hoke KR, Pletneva EV. The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c. Biochemistry 2018 Oct 9;57(40):5827-5840.
- Campelo D, Lautier T, Urban P, Esteves F, Bozonnet S, Truan G, Kranendonk M. The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength. Front Pharmacol 2017;8:755.
- Ranieri A, Millo D, Di Rocco G, Battistuzzi G, Bortolotti CA, Borsari M, Sola M. Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen. J Biol Inorg Chem 2015 Apr;20(3):531-40.
- Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C. Mitochondrial diaphorases as NAD⁺ donors to segments of the citric acid cycle that support substrate-level phosphorylation yielding ATP during respiratory inhibition. FASEB J 2014 Apr;28(4):1682-97.
- Kim N, Ripple MO, Springett R. Measurement of the mitochondrial membrane potential and pH gradient from the redox poise of the hemes of the bc1 complex. Biophys J 2012 Mar 7;102(5):1194-203.
- Tomásková N, Varhac R, Zoldák G, Oleksáková L, Sedláková D, Sedlák E. Conformational stability and dynamics of cytochrome c affect its alkaline isomerization. J Biol Inorg Chem 2007 Feb;12(2):257-66.
- Beard DA. A biophysical model of the mitochondrial respiratory system and oxidative phosphorylation. PLoS Comput Biol 2005 Sep;1(4):e36.
- Battistuzzi G, Borsari M, Ranieri A, Sola M. Solvent-based deuterium isotope effects on the redox thermodynamics of cytochrome c. J Biol Inorg Chem 2004 Sep;9(6):781-7.
- Frank J, Dijkstra M, Balny C, Verwiel PE, Duine JA. Methanol dehydrogenase: mechanism of action. Antonie Van Leeuwenhoek 1989 May;56(1):25-34.
- Loveridge KM, Olsen OD, Scherer SR, Espino-Sanchez TJ, Wienkers H, Hill CP, Kay MS, Sigala PA. A Divergent Cytochrome c in Malaria Parasites with an Anomalously Low Redox Potential. bioRxiv 2025 Dec 25;.
- Maher S, Atta S, Kamel M, A Hammam O, Okasha H. Therapeutic Potential and Mechanistic Insights of a Novel Synthetic α-Lactalbumin-Derived Peptide for the Treatment of Liver Fibrosis. J Clin Exp Hepatol 2025 May-Jun;15(3):102488.
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