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Home / Equine Research Bank / Biophys J / Proton hyperfine resonance assignments using the nuclear Ove...
Biophysical journal1987; 52(1); 101-107; doi: 10.1016/S0006-3495(87)83193-4

Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c.

Abstract: Proton hyperfine resonance assignments for cytochromes c from several species are currently being successfully pursued by several laboratories. These efforts focus mostly on the ferrous forms. In contrast to that work, we have pursued assignments of the proton hyperfine shifted resonances for horse and tuna ferricytochromes c. Our results indicate that assignments are nearly identical in those two proteins. Using the pre-steady state nuclear Overhauser effect, several additional assignments have been made for the tuna protein, whereas for the horse protein, the following protons have been assigned: heme 7, alpha CH2; heme 7, beta CH2; histidine 18, beta CH2 and alpha CH; and the methionine 80, beta CH2.
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Publication Date: 1987-07-01 PubMed ID: 3038205PubMed Central: PMC1329988DOI: 10.1016/S0006-3495(87)83193-4Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research is about the study of proton hyperfine resonance assignments in cytochromes c from horse and tuna, focusing on ferric forms unlike the prevalent studies on ferrous forms.

Understanding Proton Hyperfine Resonance

  • The core theme of the research revolves around proton hyperfine resonance assignments for cytochrome c from various species. Proton hyperfine resonance refers to the minute interaction between atomic nuclei and the localized magnetic field, which helps in understanding the electronic structure of the molecule.
  • Most of the current studies are more inclined towards the ferrous forms of these proteins, which is a state where iron is present in a divalent form. But, this study differs as it mainly focuses on the ferric forms, in which iron is present in a trivalent state.

Comparison between Horse and Tuna Cytochromes c

  • The research worked on assignments of the proton hyperfine shifted resonances for cytochromes c derived from horse and tuna. Proton hyperfine shifted resonance is a specific technique used to identify protons in biological molecules.
  • The study compared the results in these two proteins and found out that the assignments are nearly identical, suggesting common structures in the proteins from these two species.

Use of Nuclear Overhauser Effect

  • The research further sensitized the proton identification process by using the pre-steady state nuclear Overhauser effect. The nuclear Overhauser effect is a complex phenomenon in nuclear magnetic resonance (NMR) spectroscopy that provides detailed information about the structure of molecules.
  • This method provided several additional assignments for the tuna protein. However, for the horse protein, the specified protons have been assigned, enhancing the understanding of its molecular structure.

Identified Assignments

  • In the horse protein, heme 7, alpha CH2; heme 7, beta CH2; histidine 18, beta CH2 and alpha CH; and the methionine 80, beta CH2 protons were identified. Each of these assigned protons has a distinct role and location in the cytochrome structure, enhancing the comprehension of their function and potential dynamics within the protein.

Overall, the study made a significant contribution by examining proton hyperfine resonance assignments for ferric forms of Horse and Tuna cytochromes c, expanding the knowledge base beyond the commonly studied ferrous forms.

Cite This Article

APA
Satterlee JD, Moench S. (1987). Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c. Biophys J, 52(1), 101-107. https://doi.org/10.1016/S0006-3495(87)83193-4

Publication

Biophysical journal
ISSN: 0006-3495
NlmUniqueID: 0370626
Country: United States
Language: English
Volume: 52
Issue: 1
Pages: 101-107

Researcher Affiliations

Satterlee, J D
    Moench, S

      MeSH Terms

      • Animals
      • Cytochrome c Group / metabolism
      • Deuterium
      • Deuterium Oxide
      • Heme
      • Histidine
      • Horses
      • Magnetic Resonance Spectroscopy / methods
      • Methionine
      • Protein Conformation
      • Species Specificity
      • Tuna
      • Water

      Grant Funding

      • RR1081 / NCRR NIH HHS

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      Citations

      This article has been cited 4 times.
      1. Casini A, Mastrobuoni G, Terenghi M, Gabbiani C, Monzani E, Moneti G, Casella L, Messori L. Ruthenium anticancer drugs and proteins: a study of the interactions of the ruthenium(III) complex imidazolium trans-[tetrachloro(dimethyl sulfoxide)(imidazole)ruthenate(III)] with hen egg white lysozyme and horse heart cytochrome c. J Biol Inorg Chem 2007 Nov;12(8):1107-17.
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        doi: 10.1007/BF01886883pubmed: 8561853google scholar: lookup
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