Monitoring the conformational flexibility of cytochrome c at low ionic strength by 1H-NMR spectroscopy.
Abstract: Horse heart cytochrome c at pH 7 and low ionic strength is present as two conformers, as evidenced by 1H-NMR spectroscopy. The two structures have been calculated using NOE and pseudocontact shift constraints. They have the same folding patterns and are essentially equal, within the rmsd of the families. The two average structures have rmsd values of 0.049 nm and 0.093 nm for the backbone and the heavy atoms, respectively. Such a difference has been analyzed through a detailed analysis of the NOEs. It appears that the species at low ionic strength differs from the species present at high ionic strength by the displacement of some external residues, such as Gln16, Ile81 and Glu90. Other changes are monitored by the chemical shifts but they cannot be quantified at the present level of resolution. Ionic-strength-dependent structural rearrangements may be relevant with respect to the problem of molecular recognition.
Publication Date: 1998-10-06 PubMed ID: 9760164DOI: 10.1046/j.1432-1327.1998.2560271.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study investigates the molecular configurations of horse heart cytochrome c at low ionic strength, using 1H-NMR spectroscopy, identifying two conformers and analysing structural differences between the two.
Research Methodology and Findings
- In this research, scientists used 1H-NMR spectroscopy to study the structural properties of horse heart cytochrome c at pH 7 and at low ionic strength. The results led to the identification of two conformations of the molecule.
- The two structures were calculated using Nuclear Overhauser Effect (NOE) and pseudocontact shift constraints. These scientific methods allow for the investigation of spatial properties and folding patterns of molecules. The result showed that the structures have the same folding patterns and are almost equal within their comparable root-mean-square deviation (rmsd) values.
- Rmsd is used here to measure the average distance between the atoms (backbone and heavy atoms) of superimposed proteins. The two average structures exhibited rmsd values of 0.049 nm and 0.093 nm for the backbone and the heavy atoms, respectively.
- A detailed analysis of the NOEs revealed differences. These were mainly due to the displacement of some external residues like Gln16, Ile81, and Glu90. It is inferred that the species at low ionic strength differs from those at high ionic strength due to these displacements.
- Chemical shifts also monitored other changes, although they could not be quantified at the current level of resolution.
Significance of the Study
- This research is important because ionic-strength-dependent structural rearrangements can influence molecular recognition, a crucial factor in biochemistry and drug design.
- This study gives foundational insights into how the conformation of molecules such as horse heart cytochrome c can change under different ionic strengths, thus guiding future research in tailoring molecules to better fit their intended functions.
Cite This Article
APA
Banci L, Bertini I, Reddig T, Turano P.
(1998).
Monitoring the conformational flexibility of cytochrome c at low ionic strength by 1H-NMR spectroscopy.
Eur J Biochem, 256(2), 271-278.
https://doi.org/10.1046/j.1432-1327.1998.2560271.x Publication
Researcher Affiliations
- Department of Chemistry, University of Florence, Italy.
MeSH Terms
- Algorithms
- Animals
- Cytochrome c Group / chemistry
- Horses
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Myocardium / chemistry
- Osmolar Concentration
- Phosphates / metabolism
- Protein Conformation
- Protein Folding
Citations
This article has been cited 6 times.- Schweitzer-Stenner R. Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case. Molecules 2022 Dec 9;27(24).
- Lalli D, Rosa C, Allegrozzi M, Turano P. Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation. Int J Mol Sci 2020 Mar 20;21(6).
- Soffer JB, Schweitzer-Stenner R. Near-exact enthalpy-entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c. J Biol Inorg Chem 2014 Oct;19(7):1181-94.
- Muenzner J, Pletneva EV. Structural transformations of cytochrome c upon interaction with cardiolipin. Chem Phys Lipids 2014 Apr;179:57-63.
- Abriata LA, Cassina A, Tórtora V, Marín M, Souza JM, Castro L, Vila AJ, Radi R. Nitration of solvent-exposed tyrosine 74 on cytochrome c triggers heme iron-methionine 80 bond disruption. Nuclear magnetic resonance and optical spectroscopy studies. J Biol Chem 2009 Jan 2;284(1):17-26.
- Schweitzer-Stenner R. Order-to-Disorder and Disorder-to-Order Transitions of Proteins upon Binding to Phospholipid Membranes: Common Ground and Dissimilarities. Biomolecules 2025 Jan 30;15(2).
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