A comparative kinetic analysis of the reactivity of plant, horse, and human respiratory cytochrome c towards cytochrome c oxidase.
Abstract: Two synthetic genes coding for human and Arabidopsis cytochrome c, respectively, have been designed and constructed, and the recombinant proteins have been over-expressed in Escherichia coli cells. Thus a comparative analysis of the two heme proteins, including horse cytochrome c as a reference, has been performed. In addition to their physico-chemical properties, the redox behavior of the three proteins has been analyzed by following the kinetics of both their reduction by flavin semiquinones (lumiflavin, riboflavin, and FMN) and oxidation by cytochrome c oxidase. The resulting data indicate that the accessibility and electrostatic charge of the active site do not differ in a significant way among the three proteins, but human cytochrome c exhibits some intriguing differences when interacting with cytochrome c oxidase that could be related to the amino acid changes underwent by the latter along evolution.
Publication Date: 2006-06-12 PubMed ID: 16782050DOI: 10.1016/j.bbrc.2006.06.022Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article discusses a comparative study of the reaction rates of cytochrome c proteins found in plants (specifically Arabidopsis), horses, and humans when interacting with cytochrome c oxidase. Genes for Arabidopsis and human cytochrome were synthetically created, and along with horse cytochrome c, their properties, redox behaviors and interactions with cytochrome c oxidase were analyzed.
Research Methodology
- The researchers designed and constructed two synthetic genes that code for human and Arabidopsis cytochrome c.
- The recombinant proteins from these synthetic genes were over-expressed in E. Coli cells.
- They then compared these two heme proteins with horse cytochrome c, which served as a reference.
Physico-chemical Properties and Redox Behavior
- Upon engagement in comparative analysis, the researchers examined the physico-chemical properties of these proteins.
- The redox (reduction and oxidation) behavior of the three proteins was also analyzed by tracking the kinetics of their reduction by flavin semiquinones (lumiflavin, riboflavin, and FMN), and oxidation by cytochrome c oxidase.
Analysis of the Active Sites
- The data revealed that there were no significant differences between the electrostatic charge and accessibility of the active site of these three proteins.
- What the researchers found intriguing, however, was that the human cytochrome c displayed some distinct differences when interacting with cytochrome c oxidase compared to the other two.
- These differences could potentially be attributed to the changes in amino acids that the human cytochrome c oxidase underwent during the course of evolution.
The overall findings from this research may offer valuable insights into the evolutionary changes in cytochrome c and its interactions with cytochrome c oxidase in diverse life forms.
Cite This Article
APA
Rodríguez-Roldán V, García-Heredia JM, Navarro JA, Hervás M, De la Cerda B, Molina-Heredia FP, De la Rosa MA.
(2006).
A comparative kinetic analysis of the reactivity of plant, horse, and human respiratory cytochrome c towards cytochrome c oxidase.
Biochem Biophys Res Commun, 346(3), 1108-1113.
https://doi.org/10.1016/j.bbrc.2006.06.022 Publication
Researcher Affiliations
- Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y CSIC, Centro de Investigaciones Científicas Isla de la Cartuja, Sevilla, Spain.
MeSH Terms
- Animals
- Arabidopsis / enzymology
- Chemical Phenomena
- Chemistry, Physical
- Cytochromes c / metabolism
- Electron Transport Complex IV / metabolism
- Flavins / metabolism
- Horses
- Humans
- Kinetics
- Mitochondria / enzymology
- Oxidation-Reduction / drug effects
- Potassium Chloride / pharmacology
Citations
This article has been cited 10 times.- Márquez I, Pérez-Mejías G, Guerra-Castellano A, Olloqui-Sariego JL, Andreu R, Calvente JJ, De la Rosa MA, Díaz-Moreno I. Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants.. FEBS Open Bio 2021 Dec;11(12):3304-3323.
- Martínez-Fábregas J, Díaz-Moreno I, González-Arzola K, Janocha S, Navarro JA, Hervás M, Bernhardt R, Velázquez-Campoy A, Díaz-Quintana A, De la Rosa MA. Structural and functional analysis of novel human cytochrome C targets in apoptosis.. Mol Cell Proteomics 2014 Jun;13(6):1439-56.
- Martínez-Fábregas J, Díaz-Moreno I, González-Arzola K, Janocha S, Navarro JA, Hervás M, Bernhardt R, Díaz-Quintana A, De la Rosa MÁ. New Arabidopsis thaliana cytochrome c partners: a look into the elusive role of cytochrome c in programmed cell death in plants.. Mol Cell Proteomics 2013 Dec;12(12):3666-76.
- Basu S, Leonard JC, Desai N, Mavridou DA, Tang KH, Goddard AD, Ginger ML, Lukeš J, Allen JW. Divergence of Erv1-associated mitochondrial import and export pathways in trypanosomes and anaerobic protists.. Eukaryot Cell 2013 Feb;12(2):343-55.
- Millar AH, Small ID, Day DA, Whelan J. Mitochondrial biogenesis and function in Arabidopsis.. Arabidopsis Book 2008;6:e0111.
- Pierron D, Opazo JC, Heiske M, Papper Z, Uddin M, Chand G, Wildman DE, Romero R, Goodman M, Grossman LI. Silencing, positive selection and parallel evolution: busy history of primate cytochromes C.. PLoS One 2011;6(10):e26269.
- Pierron D, Wildman DE, Hüttemann M, Markondapatnaikuni GC, Aras S, Grossman LI. Cytochrome c oxidase: evolution of control via nuclear subunit addition.. Biochim Biophys Acta 2012 Apr;1817(4):590-7.
- García-Heredia JM, Díaz-Quintana A, Salzano M, Orzáez M, Pérez-Payá E, Teixeira M, De la Rosa MA, Díaz-Moreno I. Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.. J Biol Inorg Chem 2011 Dec;16(8):1155-68.
- Ying T, Zhong F, Xie J, Feng Y, Wang ZH, Huang ZX, Tan X. Evolutionary alkaline transition in human cytochrome c.. J Bioenerg Biomembr 2009 Jun;41(3):251-7.
- García-Heredia JM, Hervás M, De la Rosa MA, Navarro JA. Acetylsalicylic acid induces programmed cell death in Arabidopsis cell cultures.. Planta 2008 Jun;228(1):89-97.
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