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Home / Equine Research Bank / Biochem J / Identification of the ligand-exchange process in the alkalin...
The Biochemical journal1987; 246(1); 43-54; doi: 10.1042/bj2460043

Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c.

Abstract: Magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K of horse heart cytochrome c are reported at a series of pH values between 7.8 and 11.0, encompassing the alkaline transition. The effect of glassing agents on the e.p.r. spectrum at various pH values is also reported. Comparison of these results with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin support the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c. The m.c.d. and e.p.r. spectra of horse heart cytochrome c in the presence of 1-methylimidazole have also been examined. These studies strongly suggest that histidine-18, the proximal ligand of the haem, is the ionizing group that triggers the alkaline transition. Low-temperature m.c.d. and e.p.r. spectra are also reported for Pseudomonas aeruginosa cytochrome c551. It is shown that no ligand exchange takes place at the haem in this species over the pH range 6.0-11.3.
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Publication Date: 1987-08-15 PubMed ID: 2823795PubMed Central: PMC1148238DOI: 10.1042/bj2460043Google Scholar: Lookup
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  • Journal Article
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  • Non-U.S. Gov't

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.

This research investigates the ligand-exchange process in the alkaline transition of horse heart cytochrome c, examining the impacts of pH on magnetic-circular-dichroism (m.c.d.) spectra. The findings strongly suggest that histidine-18 is the triggering group for this transition.

Understanding Cytochrome C and Ligand-Exchange Process

  • The research revolves around Cytochrome c, a small protein found in many living organisms, which plays a crucial role in the process of cellular respiration.
  • It is involved in the transport of electrons during the production of energy in cells.
  • The “ligand-exchange process” refers to the swapping of one ligand (an ion or molecule that binds to a central atom to form a coordination complex) for another within a molecule.

Methodology and Experiments

  • The team conducted a survey of magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K for horse heart cytochrome c at various pH levels (7.8 to 11.0).
  • They compared the effects of different glassing agents on the electron paramagnetic resonance (e.p.r.) spectrum at these pH levels.
  • The results were then compared with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin, aiding in the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c.
  • The team also studied the m.c.d. and e.p.r. spectra of horse heart cytochrome c in the presence of 1-methylimidazole.

Key Findings

  • These investigations strongly suggest that histidine-18 is the proximal ligand of the haem (an iron-containing compound that forms the non-protein part of certain enzymes) and is responsible for triggering the alkaline transition.
  • In contrast, the research observed that no ligand exchange occurs in the haem of Pseudomonas aeruginosa cytochrome c551 over the pH range 6.0-11.3, showing a diverse range of reactions in different species.

Cite This Article

APA
Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ. (1987). Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. Biochem J, 246(1), 43-54. https://doi.org/10.1042/bj2460043

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 246
Issue: 1
Pages: 43-54

Researcher Affiliations

Gadsby, P M
  • School of Chemical Sciences, University of East Anglia, Norwich, U.K.
Peterson, J
    Foote, N
      Greenwood, C
        Thomson, A J

          MeSH Terms

          • Animals
          • Bacterial Proteins
          • Circular Dichroism
          • Cytochrome c Group
          • Electron Spin Resonance Spectroscopy
          • Horses
          • Hydrogen-Ion Concentration
          • Imidazoles
          • Ligands
          • Myocardium / enzymology
          • Pseudomonas aeruginosa / analysis
          • Temperature

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          Citations

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