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Home / Equine Research Bank / Proc Natl Acad Sci U S A / Reduction of ferricytochrome c by dithionite ion: electron t...
Proceedings of the National Academy of Sciences of the United States of America1973; 70(6); 1701-1703; doi: 10.1073/pnas.70.6.1701

Reduction of ferricytochrome c by dithionite ion: electron transfer by parallel adjacent and remote pathways.

Abstract: The kinetics of the reduction of horseheart ferricytochrome c by sodium dithionite (phosphate buffer-sodium chloride; pH 6.5, mu = 1.0, 25 degrees ) features two reaction pathways; one with the rate constant k(3) = 1.17 x 10(4) M(-1) sec(-1), the other with the rate constant k(1)k(2)/k(-1) = 6.0 x 10(4) M(-1) sec(-1). These pathways are interpreted in terms of remote attack (possibly by way of the exposed edge of the porphyrin system) and adjacent attack (requiring the opening of the heme crevice). The limiting rate for the adjacent pathway (k(1) = 30 sec(-1)) is in good agreement with the rate of heme-crevice opening of ferricytochrome c determined in other studies. The implication of the adjacent attack pathway to the function of cytochrome c in vivo is discussed.
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Publication Date: 1973-06-01 PubMed ID: 4352650PubMed Central: PMC433576DOI: 10.1073/pnas.70.6.1701Google 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.

This research article investigates the process of electron transition in a certain molecule, specifically observing two distinct pathways. The researchers measured the reaction speeds of each pathway, noting their relation to the structural characteristics of the molecular system.

Characterization of two reaction pathways

  • The researchers, while studying the reaction kinetics of the reduction of horseheart ferricytochrome c, identified two pathways that the reaction could take. Ferricytochrome c is a specific form of the molecule cytochrome c, which plays crucial roles in all aerobic life forms, assisting in cellular metabolism.
  • These pathways are defined by the area of the molecule with which the electron interact – one pathway involves the ‘adjacent’ attack and another involves a ‘remote’ attack.

    • Measurement of the reaction speed of each pathway

    • Each pathway features its own distinct rate constant – a measure of the speed of the reaction. The ‘adjacent’ attack pathway has a rate constant of 1.17 x 10(4) M(-1) sec(-1), whereas the ‘remote’ attack pathway features a different rate constant – k(1)k(2)/k(-1) = 6.0 x 10(4) M(-1) sec(-1).
    • The limiting rate for the adjacent pathway (k(1) = 30 sec(-1)) matches the rate of heme-crevice opening of ferricytochrome c. Here, the ‘heme-crevice’ refers to a part of the molecular structure, which the molecule needs to open to allow the electron through. The rate of this ‘opening’ process matches that of the adjacent pathway, indicating that this structural characteristic is the limiting factor of the reaction.

      • Implications for our understanding of cytochrome c’s function

      • The study’s findings suggest that the ‘adjacent’ attack pathway could be connected to the real-world function of cytochrome c inside a living organism.
      • As such, this research helps clarify how cytochrome c conducts its crucial life-sustaining metabolism assistance functions, and thereby provides new insights into the workings of aerobic life forms at the molecular level.

Cite This Article

APA
Creutz C, Sutin N. (1973). Reduction of ferricytochrome c by dithionite ion: electron transfer by parallel adjacent and remote pathways. Proc Natl Acad Sci U S A, 70(6), 1701-1703. https://doi.org/10.1073/pnas.70.6.1701

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: 70
Issue: 6
Pages: 1701-1703

Researcher Affiliations

Creutz, C
    Sutin, N

      MeSH Terms

      • Animals
      • Cytochrome c Group
      • Electron Transport
      • Horses
      • Iron
      • Kinetics
      • Myocardium / enzymology
      • Oxidation-Reduction
      • Protein Conformation
      • Structure-Activity Relationship
      • Sulfites

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