Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: the role of His-E7 and Val-E11.
Abstract: Electron nuclear double resonance (ENDOR) spectroscopy has been used to study protons in nitrosyl horse heart myoglobin (MbNO). (1)H ENDOR spectra were recorded for different settings of the magnetic field. Detailed analysis of the ENDOR powder spectra, using computer simulation, based on the "orientation-selection" principle, leads to the identification of the available protons in the heme pocket. We observe hyperfine interactions of the N(HisF8)-Fe(2+)-N(NO) complex with five protons in axial and with eight protons in the rhombic symmetry along different orientations, including those of the principal axes of the g-tensor. Protons from His-E7 and Val-E11 residues are identified in the two symmetries, rhombic and axial, exhibited by MbNO. Our results indicate that both residues are present inside the heme pocket and help to stabilize one particular conformation.
Publication Date: 2000-03-29 PubMed ID: 10733988PubMed Central: PMC1300802DOI: 10.1016/S0006-3495(00)76757-9Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research uses a technique called electron nuclear double resonance to investigate the proteins found in horse heart myoglobin, particularly the proton interactions. The findings suggest that certain residues help to stabilize the structure of the protein.
Research Methodology
- The study employed Electron Nuclear Double Resonance (ENDOR) spectroscopy, a technique often used to examine unobserved nuclear spins in the vicinity of a paramagnetic center. In this context, the technique was used to study protons in nitrosyl horse heart myoglobin (MbNO).
- The researchers recorded (1)H ENDOR spectra for different settings of the magnetic field. This helps to measure the magnetic properties of the protons within the protein.
- They also utilized computer simulations based on the “orientation-selection” principle, that enables them to clearly identify and analyze the available protons in the heme pocket, a cavity within the protein.
Findings and Conclusion
- Through their detailed analysis of the ENDOR powder spectra, the team was able to identify hyperfine interactions of the N(HisF8)-Fe(2+)-N(NO) complex with numerous protons in both axial and rhombic symmetries along different orientations.
- The researchers identified protons from two residues called His-E7 and Val-E11 in both the Rhombic and Axial symmetries. These residues are structural subunits of proteins.
- The team concluded that these residues are present inside the heme pocket, which suggests that they play an important role in stabilizing a particularly significant protein formation.
Cite This Article
APA
Flores M, Wajnberg E, Bemski G.
(2000).
Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: the role of His-E7 and Val-E11.
Biophys J, 78(4), 2107-2115.
https://doi.org/10.1016/S0006-3495(00)76757-9 Publication
Researcher Affiliations
- Centro Brasileiro de Pesquisas Físicas, 22290-180 Rio de Janeiro, Brazil.
MeSH Terms
- Animals
- Biophysical Phenomena
- Biophysics
- Electron Spin Resonance Spectroscopy / methods
- Heme / chemistry
- Histidine / chemistry
- Horses
- Models, Molecular
- Myocardium / chemistry
- Myoglobin / chemistry
- Protein Conformation
- Protons
- Valine / chemistry
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This article includes 21 references
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Citations
This article has been cited 1 times.- Merchant KA, Noid WG, Akiyama R, Finkelstein IJ, Goun A, McClain BL, Loring RF, Fayer MD. Myoglobin-CO substate structures and dynamics: multidimensional vibrational echoes and molecular dynamics simulations.. J Am Chem Soc 2003 Nov 12;125(45):13804-18.
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