The 2.03 signal as an indicator of dinitrosyl-iron complexes with thiol-containing ligands.
Abstract: The parameters of EPR signal from dinitrosyl-iron complexes (DNIC) with bovine serum albumin (BSA), horse hemoglobin (Hb), and apometallothionein (apo-Mt) of horse kidney incorporating one (BSA, Hb) or two thiol-containing ligands (apo-Mt) were compared. The EPR signal from DNIC-BSA was characterized by the rhombic symmetry of g tensor at room temperature of signal recording (ambient temperature) or at 77K in the solution frozen in the presence of glycerol. In freezing of the solution in the absence of glycerin, under the exposure of DNIC-BSA to negatively charged sodium dodecyl sulfate (SDS) ions, or in the incorporation of DNIC-BSA into the reversed micelles formed by negatively charged ions of surfactant aerosol OT, the symmetry of the g tensor of DNIC-BSA EPR signal increased to axial. A similarly high symmetry of g tensor was observed for the DNIC-Hb EPR signal in the absence of any influence on this protein complex. The shape of EPR signals from these preparations recorded at 77K was identical to that of EPR signal from DNIC with cysteine in frozen solution. In this connection it was concluded that the EPR signal from this low-molecular DNIC with the (RS-)2Fe+(NO+)2 structure cannot be considered as a peculiar "fingerprint" of DNIC with the same structure in biosystems. In such systems the same signal can originate from protein DNIC incorporating only one thiol-containing ligand along with a nonthiol ligand. The EPR signal displayed by DNIC with apo-Mt with a high content of cysteine residues at room temperature of registration was identical to the EPR signal from frozen solution of DNIC with cysteine. This protein DNIC is apparently characterized by the same structure as DNIC with cysteine.
Publication Date: 1998-12-16 PubMed ID: 9851363DOI: 10.1006/niox.1998.0180Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article discusses a comparative analysis of Electron Paramagnetic Resonance (EPR) signals from dinitrosyl-iron complexes (DNIC) with different thiol-containing ligands. The findings indicate that the EPR signal from a low-molecular DNIC can originate from different protein DNIC in various biosystems, signalling similarities in their structural attributes.
Methodology and Analysis
- The researchers investigated the EPR signal parameters from DNIC in conjunction with bovine serum albumin (BSA), horse hemoglobin (Hb), and apometallothionein (apo-Mt) of horse kidney, which integrate one (BSA, Hb) or two thiol-containing ligands (apo-Mt).
- The specific signal from DNIC-BSA showed a rhombic symmetry of the g tensor and was established at room temperature or at 77 Kelvin (K) in a frozen solution. This experiment was conducted both under ambient temperature and in the presence of glycerol.
- The symmetry of the g tensor for the DNIC-BSA EPR signal increased to axial under certain conditions – freezing the solution without glycerin, subjecting DNIC-BSA to negatively charged sodium dodecyl sulfate (SDS) ions, or integrating DNIC-BSA into reversed micelles formed by negatively charged ions of surfactant aerosol OT.
- Contrarily, a similar high symmetry of g tensor was observed for DNIC-Hb EPR signal without any external influence on the protein complex.
Findings and Implications
- The researchers noted that the EPR signals from these experiments recorded at 77K were identical to the EPR signal from DNIC with cysteine in frozen solution.
- This similarity led to the conclusion that the EPR signal from low-molecular DNIC cannot be distinctively recognized as a specific “fingerprint” of DNIC with a similar structure in biosystems.
- It was inferred that in these biosystems, a similar signal could also emerge from a protein DNIC that incorporates only one thiol-containing ligand along with a nonthiol ligand.
- The EPR signal displayed by DNIC with apo-Mt, which has a high cysteine content, was identical to that of the frozen solution of DNIC with cysteine. This inferred that the protein DNIC seemingly possesses the same structure as DNIC with cysteine.
Overall, these findings elucidate that the EPR signal of different DNIC biosystems can potentially have identical or similar EPR signal structures under specified conditions. This could aid in enhancing our understanding of these complexes and pave the way for future research in this domain.
Cite This Article
APA
Vanin AF, Serezhenkov VA, Mikoyan VD, Genkin MV.
(1998).
The 2.03 signal as an indicator of dinitrosyl-iron complexes with thiol-containing ligands.
Nitric Oxide, 2(4), 224-234.
https://doi.org/10.1006/niox.1998.0180 Publication
Researcher Affiliations
- Institute of Chemical Physics, Russian Academy of Sciences, Moscow. mikoyan@center.chph.ras.ru
MeSH Terms
- Ammonium Sulfate / pharmacology
- Animals
- Cattle
- Cysteine / analogs & derivatives
- Cysteine / chemistry
- Dioctyl Sulfosuccinic Acid / pharmacology
- Electron Spin Resonance Spectroscopy
- Freezing
- Glutathione / chemistry
- Hemoglobins / chemistry
- Horses
- Iron / chemistry
- Metallothionein / chemistry
- Nitrogen Oxides / chemistry
- Serum Albumin / chemistry
- Sodium Dodecyl Sulfate / pharmacology
- Sulfhydryl Compounds / chemistry
Citations
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