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1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse, and sperm whale deoxy myoglobins.
Abstract: 1H-NMR spectra of deoxy myoglobins (Mbs) from shark (Galeorhinus japonicus), horse, and sperm whale have been studied to gain insights into their active site structure. It has been demonstrated for the first time that nuclear Overhauser effect (NOE) can be observed between heme peripheral side-chain proton resonances of these paramagnetic complexes. Val-E11 methyl and His-F8 C delta H proton resonances of these Mbs were also assigned from the characteristic shift and line width. The hyperfine shift of the former resonance was used to calculate the magnetic anisotropy of the protein. The shift analysis of the latter resonance, together with the previously assigned His-F8 N delta H proton resonance, revealed that the strain on the Fe-N epsilon bond is in the order horse Mb approximately whale Mb < shark Mb and that the hydrogen bond strength of the His-F8 N delta H proton to the main-chain carbonyl oxygen in the preceding turn of the F helix is in the order shark Mb < horse Mb < whale Mb. Weaker Feporphyrin interaction in shark Mb was manifested in a smaller shift of the heme methyl proton resonance and appears to result from distortion of the coordination geometry in this Mb. Larger strain on the Fe-N epsilon bond in shark Mb should be to some extent attributed to its lowered O2 affinity (P50 = 1.1 mmHg at 20 degrees C), compared to whale and horse Mbs.
Publication Date: 1992-09-01 PubMed ID: 1429532DOI: 10.1093/oxfordjournals.jbchem.a123914Google Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Comparative Study
- Journal Article
Summary
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The research article presents a comparative study of the active site (the region of an enzyme where substrate molecules bind and undergo a chemical reaction) in deoxy myoglobins (a form of protein in muscle cells that releases oxygen) from sharks (Galeorhinus japonicus), horses, and sperm whales using 1H-NMR (a type of nuclear magnetic resonance spectroscopy) and explores the differences in structural and bonding characteristics among these species.
Objective of the Study
- The aim of the research was to analyze the 1H-NMR spectra of deoxy myoglobins from sharks, horses, and sperm whales in order to understand their active site structure and gain insights into fundamental protein behavior across different species.
Methods Used
- The research utilized nuclear Overhauser effect (a phenomenon in nuclear magnetic resonance spectroscopy) to observe interactions between heme peripheral side-chain proton resonances in these complexes.
- Val-E11 methyl and His-F8 C delta H proton resonances of these myoglobins were also studied and assigned based on characteristic shift and line width.
- The hyperfine shift of the Val-E11 methyl resonance was used to calculate the magnetic anisotropy of the protein.
Key Findings
- The strain on the Fe-N epsilon bond (a bond between the iron atom and the nitrogen atom in the heme group of the protein) varied in order: horse myoglobin ≈ whale myoglobin < shark myoglobin.
- The hydrogen bond strength of the His-F8 N delta H proton to the main-chain carbonyl oxygen was found to vary in the opposite order: shark myoglobin < horse myoglobin < whale myoglobin.
- NMR analysis revealed that the shark myoglobin exhibited weaker Feporphyrin interaction as compared to horse and whale myoglobin.
- Distortion of the coordination geometry in shark myoglobin appears to be responsible for the observed weaker Feporphyrin interaction.
- The strain on the Fe-N epsilon bond was relatively larger in shark myoglobin and may be attributed to the lower O2 affinity of shark myoglobin.
Implications of the Study
- These findings can help further our understanding of the variations in molecular architecture and function across different proteins and species.
- Understanding these protein structures in detail can provide valuable insights into their biological function and may have potential applications in bioengineering and the pharmaceutical industry.
Cite This Article
APA
Yamamoto Y, Iwafune K, Chûjô R, Inoue Y, Imai K, Suzuki T.
(1992).
1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse, and sperm whale deoxy myoglobins.
J Biochem, 112(3), 414-420.
https://doi.org/10.1093/oxfordjournals.jbchem.a123914 Publication
Researcher Affiliations
- Department of Biomolecular Engineering, Tokyo Institute of Technology.
MeSH Terms
- Animals
- Binding Sites
- Heme / chemistry
- Horses
- Magnetic Resonance Spectroscopy
- Molecular Structure
- Myoglobin / chemistry
- Myoglobin / metabolism
- Oxygen / metabolism
- Porphyrins / chemistry
- Sharks
- Species Specificity
- Temperature
- Whales
Citations
This article has been cited 1 times.- Yamamoto Y, Nagao S, Hirai Y, Inose T, Terui N, Mita H, Suzuki A. NMR investigation of the heme electronic structure in deoxymyoglobin possessing a fluorinated heme. J Biol Inorg Chem 2004 Mar;9(2):152-60.
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