ArticleProtein science : a publication of the Protein Society2009
Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 41 citations in OpenAlex.
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Binding of yeast and human cytochrome c to cardiolipin nanodiscs at physiological ionic strength.Journal of inorganic biochemistry · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Effect on intrinsic peroxidase activity of substituting coevolved residues from Ω-loop C of human cytochrome c into yeast iso-1-cytochrome c.Journal of inorganic biochemistry · 2022Article
- Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.Biochemistry · 2021Article
- How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing.Molecules (Basel, Switzerland) · 2021Review
- The Human CytochromeBiochemistry · 2020Article
- Quantitative Photo-crosslinking Mass Spectrometry Revealing Protein Structure Response to Environmental Changes.Analytical chemistry · 2019Article
- The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.Biochemistry · 2018Article
- Ligation and Reactivity of Methionine-Oxidized Cytochrome c.Inorganic chemistry · 2018Article
- Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Biochemistry · 2017Article
- Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Journal of the American Chemical Society · 2016Article
- Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability.Journal of inorganic biochemistry · 2016Article
- The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Article
- Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural transformations of cytochrome c upon interaction with cardiolipin.Chemistry and physics of lipids · 2014Review
- Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c.The journal of physical chemistry. B · 2013Article
- Dynamics of the His79-heme alkaline transition of yeast iso-1-cytochrome c probed by conformationally gated electron transfer with Co(II)bis(terpyridine).Journal of the American Chemical Society · 2013Article
- Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
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3 authors at 1 institution in 1 country.
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Abstract
Evolutionary conservation of substructure architecture between yeast iso-1-cytochrome c and the well-characterized horse cytochrome c is studied with limited proteolysis, the alkaline conformational transition and global unfolding with guanidine-HCl. Mass spectral analysis of limited proteolysis cleavage products for iso-1-cytochrome c show that its least stable substructure is the same as horse cytochrome c. The limited proteolysis data yield a free energy of 3.8 +/- 0.4 kcal mol(-1) to unfold the least stable substructure compared with 5.05 +/- 0.30 kcal mol(-1) for global unfolding of iso-1-cytochrome c. Thus, substructure stabilities of iso-1-cytochrome c span only approximately 1.2 kcal mol(-1) compared with approximately 8 kcal mol(-1) for horse cytochrome c. Consistent with the less cooperative folding thus expected for the horse protein, the guanidine-HCl m-values are approximately 3 kcal mol(-1)M(-1) versus approximately 4.5 kcal mol(-1)M(-1) for horse versus yeast cytochrome c. The tight free energy spacing of the yeast cytochrome c substructures suggests that its folding has more branch points than for horse cytochrome c. Studies on a variant of iso-1-cytochrome c with an H26N mutation indicate that the least and most stable substructures unfold sequentially and the two least stable substructures unfold independently as for horse cytochrome c. Thus, important aspects of the substructure architecture of horse cytochrome c, albeit compressed energetically, are preserved evolutionally in yeast iso-1-cytochrome c.
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