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The impact of urea-induced unfolding on the redox process of immobilised cytochrome \<i\>c\</i\>
Citation key Monari2010
Author Monari, Stefano and Millo, Diego and Ranieri, Antonio and Di Rocco, Giulia and van der Zwan, Gert and Gooijer, Cees and Peressini, Silvia and Tavagnacco, Claudio and Hildebrandt, Peter and Borsari, Marco
Pages 1233-1242
Year 2010
ISSN 0949-8257
Journal Journal of Biological Inorganic Chemistry
Volume 15
Note 10.1007/s00775-010-0681-7
Publisher Springer Berlin / Heidelberg
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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