2009
DOI: 10.1007/s10800-009-9804-7
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Redox thermodynamics of cytochromes c subjected to urea induced unfolding

Abstract: The thermodynamics of the electron transfer (ET) process for beef heart and yeast cytochromes c and the Lys72Ala/Lys73Ala/Lys79Ala mutant of the latter species subjected to progressive urea-induced unfolding was determined electrochemically. The results indicate the presence of at least three protein forms which were assigned to a low-temperature and a high-temperature HisMet intermediate species and a bis-histidinate form (although the presence of a His-Lys form cannot be excluded). The much lower E°0 value o… Show more

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Cited by 12 publications
(22 citation statements)
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References 61 publications
(156 reference statements)
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“…2). Conversely, the respective transitions in solution are found at 3.5 and 3.2 M for ycc and K72AK73AK79A, respectively [44]. Thus, we conclude that Lys72, Lys73 and Lys79 stabilise the protein structure in the adsorbed state.…”
Section: Thermodynamics Of the Interfacial Redox Processmentioning
confidence: 66%
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“…2). Conversely, the respective transitions in solution are found at 3.5 and 3.2 M for ycc and K72AK73AK79A, respectively [44]. Thus, we conclude that Lys72, Lys73 and Lys79 stabilise the protein structure in the adsorbed state.…”
Section: Thermodynamics Of the Interfacial Redox Processmentioning
confidence: 66%
“…The solution contained 5 mM sodium perchlorate and 5 mM phosphate buffer (pH 7, T = 278 K). The spectra were obtained with 413-nm excitation which exhibits the same haem pocket structure as B1 [38], and for cytochrome c in urea-containing solution [36,41,43,44] and is consistent with a change of the ligand from S-Met to N-His [3,35,36,47]. The difference in the reduction potential, DE°0, between these two states is 0.031 V more positive for ycc than for K72AK73AK79A ( Table 2).…”
Section: Thermodynamics Of the Interfacial Redox Processmentioning
confidence: 71%
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