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Springer Verlag, Journal of Applied Electrochemistry, 11(39), p. 2181-2190

DOI: 10.1007/s10800-009-9804-7

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Redox thermodynamics of cytochromes c subjected to urea induced unfolding

Journal article published in 2009 by Stefano Monari, Antonio Ranieri, Giulia Di Rocco ORCID, Gert van der Zwan, Silvia Peressini, Claudio Tavagnacco, Diego Millo, Marco Borsari
This paper is available in a repository.
This paper is available in a repository.

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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 His- Met intermediate species and a bis-histidinate form (although the presence of a His-Lys form cannot be excluded)