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Conformational substates of horse heart cytochrome c exhibit different thermal unfolding of the heme cavity
Journal article

Conformational substates of horse heart cytochrome c exhibit different thermal unfolding of the heme cavity

Reinhard Schweitzer-Stenner, Ronak Shah, Andrew Hagarman and Isabelle Dragomir
The journal of physical chemistry. B, v 111(32), pp 9603-9607
16 Aug 2007
DOI: https://doi.org/10.1021/jp069022j
PMID: 17628093
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Cytochromes c - chemistry Myocardium - enzymology Temperature Animals Myocardium - chemistry Protein Denaturation Horses Protein Conformation Protein Folding
The charge transfer (CT) band at 695 nm in the spectrum of ferri-cytochrome c is highly asymmetric, indicating conformational heterogeneity due to the coexistence of different conformational substates. We have measured the respective band profile of horse heart ferri-cytochrome c as a function of temperature between 283 K (10 degrees C) and 333 K (60 degrees C) and found that the well-known decrease of the absorptivity is wavenumber-dependent and exhibits a biphasic behavior. This indicates that the underlying conformational substates differ in their thermodynamic stability with respect to the structural changes associated with the disappearance of the 695 nm band, which eventually (at high temperatures) involves the replacement of M80 by a nearby lysine residue. Our data further indicates that the thermal unfolding process involves two structurally different intermediate states.

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18 citations in Web of Science
19 citations in Scopus

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Web of Science research areas
Biophysics
Chemistry, Physical
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