ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2010
The impact of urea-induced unfolding on the redox process of immobilised cytochrome c.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 31 citations in OpenAlex.
- Effect of urea as a chaotropic agent on self-association of organic molecules in aqueous flow batteries.Physical chemistry chemical physics : PCCP · 2026Article
- Phosphorylation disrupts long-distance electron transport in cytochrome c.Nature communications · 2022Article
- Assessing the Functional and Structural Stability of the Met80Ala Mutant of CytochromeMolecules (Basel, Switzerland) · 2022Article
- How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing.Molecules (Basel, Switzerland) · 2021Review
- Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Identification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterization.Journal of the American Chemical Society · 2014Article
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Authors and funding
10 authors at 4 institutions in 3 countries.
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Abstract
We have studied the effect of urea-induced unfolding on the electron transfer process of yeast iso-1-cytochrome c and its mutant K72AK73AK79A adsorbed on electrodes coated by mixed 11-mercapto-1-undecanoic acid/11-mercapto-1-undecanol self-assembled monolayers. Electrochemical measurements, complemented by surface enhanced resonance Raman studies, indicate two distinct states of the adsorbed proteins that mainly differ with respect to the ligation pattern of the haem. The native state, in which the haem is axially coordinated by Met80 and His18, displays a reduction potential that slightly shifts to negative values with increasing urea concentration. At urea concentrations higher than 6 M, a second state prevails in which the Met80 ligand is replaced by an additional histidine residue. This structural change in the haem pocket is associated with an approximately 0.4 V shift of the reduction potential to negative values. These two states were found for both the wild-type protein and the mutant in which lysine residues 72, 73 and 79 had been substituted by alanines. The analysis of the reduction potentials, the reaction enthalpies and entropies as well as the rate constants indicates that these three lysine residues have an important effect on stabilising the protein structure in the adsorbed state and facilitating the electron transfer dynamics.
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