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Proceedings of the National Academy of Sciences of the United States of America1974; 71(7); 2892-2894; doi: 10.1073/pnas.71.7.2892

Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.

Abstract: Changes in the visible absorbance spectra of complexes of horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts are compared with those characteristic of native and fully guanidinated ferricytochrome c over the pH range 7 to 11. Upon raising the pH, the methionine ligand in the guanidinated hemopeptide 1-65.peptide 66-104 complex is replaced by a strong field ligand. By contrast, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 is replaced by a weak field ligand. These results demonstrate that lysine 13 does not ligate with the heme iron upon isomerization of ferricytochrome c and that the ligand in the horse heart protein is one of the eight lysine residues in the 66-104 segment of the polypeptide, most likely lysine 79.
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Publication Date: 1974-07-01 PubMed ID: 4368392PubMed Central: PMC388578DOI: 10.1073/pnas.71.7.2892Google Scholar: Lookup
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  • Journal Article

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 examines changes in the structure of certain proteins and peptides in horse heart cytochrome c as the environment’s pH level increases from neutral to alkaline. The study found that the proteins altered their structure by replacing certain ligands, and this process did not involve a particular type of protein known as Lysine 13.

Research Details and Methods

  • The research focused on observing changes within the visible absorbance spectra of various protein complexes. These included horse heart cytochrome c hemopeptide 1-65, peptide 66-104, and their guanidinated counterparts.
  • The studies aimed at finding out how the aforementioned complexes reacted to a pH range of 7 to 11. In essence, this range shifts from a neutral to an alkaline pH.

Main Findings

  • The researchers discovered that the nature and kind of ligand in these protein complexes changed upon the increase in pH. A ligand, in this context, refers to a molecule that binds to a central metal atom to form a complex.
  • In the guanidinated hemopeptide 1-65.peptide 66-104 complex, the methionine ligand was replaced by a strong field ligand. On the other hand, the methionine ligand in the hemopeptide 1-65.guanidinated peptide 66-104 complex was replaced by a weak field ligand.
  • From these findings, it’s clear that lysine 13, a type of amino acid present in these protein complexes, does not bind with the heme iron during the structural transformation (isomerization) of ferricytochrome c.
  • The study further suggests that the new ligand in the protein complex is likely one of the eight lysine residues situated in the 66-104 segment of the polypeptide, most likely lysine 79.

Significance of the Research

  • This research helps deepen the understanding of the biochemical reaction involving ferricytochrome c, an essential protein complex found in the mitochondria of many organisms.
  • The findings might have far-reaching implications in multiple fields, including molecular biology, biochemistry, and potentially, in medical research aimed at unraveling the role of proteins in disease development and treatment.

Cite This Article

APA
Wilgus H, Stellwagen E. (1974). Alkaline isomerization of ferricytochrome c: identification of the lysine ligand. Proc Natl Acad Sci U S A, 71(7), 2892-2894. https://doi.org/10.1073/pnas.71.7.2892

Publication

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
NlmUniqueID: 7505876
Country: United States
Language: English
Volume: 71
Issue: 7
Pages: 2892-2894

Researcher Affiliations

Wilgus, H
    Stellwagen, E

      MeSH Terms

      • Animals
      • Cytochrome c Group / metabolism
      • Guanidines
      • Heme
      • Horses
      • Hydrogen-Ion Concentration
      • In Vitro Techniques
      • Iron / metabolism
      • Ligands
      • Lysine
      • Methionine
      • Myocardium / metabolism
      • Spectrophotometry, Ultraviolet

      References

      This article includes 15 references
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      Citations

      This article has been cited 4 times.
      1. Dutta A, Tapio K, Suma A, Mostafa A, Kanehira Y, Carnevale V, Bussi G, Bald I. Molecular states and spin crossover of hemin studied by DNA origami enabled single-molecule surface-enhanced Raman scattering. Nanoscale 2022 Nov 17;14(44):16467-16478.
        doi: 10.1039/d2nr03664apubmed: 36305892google scholar: lookup
      2. Wallace CJ. Modulation of the alkaline transition in cytochrome c and cytochrome c-T by full or specific partial acetimidylation. Biochem J 1984 Feb 1;217(3):601-4.
        doi: 10.1042/bj2170601pubmed: 6324740google scholar: lookup
      3. Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ. Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. Biochem J 1987 Aug 15;246(1):43-54.
        doi: 10.1042/bj2460043pubmed: 2823795google scholar: lookup
      4. Pettigrew GW, Aviram I, Schejter A. Physicochemical properties of two atypical cytochromes c, Crithidia cytochrome c-557 and Euglena cytochrome c-558. Biochem J 1975 Jul;149(1):155-67.
        doi: 10.1042/bj1490155pubmed: 242319google scholar: lookup
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