ArticleEuropean biophysics journal : EBJ2003
Conformational equilibria and dynamics of cytochrome c induced by binding of sodium dodecyl sulfate monomers and micelles.
Article in European biophysics journal : EBJ, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Kinetics of Structural Transitions Induced by Sodium Dodecyl Sulfate in α-Chymotrypsin.ACS omega · 2023Article
- Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins.Biomolecules · 2023Review
- Redox Epiphospholipidome in Programmed Cell Death Signaling: Catalytic Mechanisms and Regulation.Frontiers in endocrinology · 2020Review
- Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control.Molecules (Basel, Switzerland) · 2018Review
- Long-term protein packaging in bio-ionic liquids: Improved catalytic activity and enhanced stability of cytochrome C against multiple stresses.Green chemistry : an international journal and green chemistry resource : GC · 2017Article
- Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Structural transformations of cytochrome c upon interaction with cardiolipin.Chemistry and physics of lipids · 2014Review
- Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- The non-native conformations of cytochrome c in sodium dodecyl sulfate and their modulation by ATP.European biophysics journal : EBJ · 2011Article
- Extended cardiolipin anchorage to cytochrome c: a model for protein-mitochondrial membrane binding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- Probing early events in ferrous cytochrome c folding with time-resolved natural and magnetic circular dichroism spectroscopies.Current protein & peptide science · 2009Review
- Spectroscopic, structural, and functional characterization of the alternative low-spin state of horse heart cytochrome C.Biophysical journal · 2008Article
- Multiphasic kinetics of myoglobin/sodium dodecyl sulfate complex formation.Biophysical journal · 2007Article
- Heme coordination states of unfolded ferrous cytochrome C.Biophysical journal · 2006Article
- ATP specifically drives refolding of non-native conformations of cytochrome c.Protein science : a publication of the Protein Society · 2005Article
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Authors and funding
3 authors.
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Abstract
Circular dichroism, nuclear magnetic resonance, electron paramagnetic resonance, UV-vis absorption, and resonance Raman (RR) spectroscopic techniques were employed to study protein and heme structural changes of cytochrome c (Cyt-c) induced by sodium dodecyl sulfate (SDS) monomers and micelles via hydrophobic and electrostatic interactions, respectively. Both modes of interactions cause the transition to the conformational state B2, which is implicated to be involved in the physiological processes of Cyt-c. At sub-micellar concentrations of SDS, specific binding of only ca. three SDS monomers, which is likely to occur at the hydrophobic peptide segment 81-85, is sufficient for a complete conversion to a B2 state in which Met80 is replaced by His33 (His26). These heme pocket structural changes are not linked to secondary structure changes of the protein brought about by nonspecific binding of SDS monomers in different regions of the protein. Upon binding of micelles, B2 high-spin species can also be stabilized by electrostatic interactions. In addition, the micelle interaction domain is located on the front surface of Cyt-c, which includes a ring-like arrangement of lysine residues appropriate for binding one micelle. According to freeze-quench RR and stopped-flow experiments, state B2 is formed on the long millisecond timescale and reveals a complex dependence on the SDS concentration that can be interpreted in terms of competitive binding of monomers and micelles.
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