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Home / Equine Research Bank / Biophys J / The transition from inhomogeneous to homogeneous kinetics in...
Biophysical journal1994; 66(5); 1612-1622; doi: 10.1016/S0006-3495(94)80953-1

The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin.

Abstract: Heme proteins react inhomogeneously with ligands at cryogenic temperatures and homogeneously at room temperature. We have identified and characterized a transition from inhomogeneous to homogeneous behavior at intermediate temperatures in the time dependence of CO binding to horse myoglobin. The turnover is attributed to a functionally important tertiary protein relaxation process during which the barrier increases dynamically. This is verified by a combination of theory and multipulse measurements. A likely biological significance of this effect is in the autocatalysis of the ligand release process.
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Publication Date: 1994-05-01 PubMed ID: 8061210PubMed Central: PMC1275881DOI: 10.1016/S0006-3495(94)80953-1Google 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.

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 discusses the transition from inhomogeneous to homogeneous kinetics in myoglobin’s reaction with carbon monoxide (CO), highlighting how the behavior changes with different temperatures, and its possible biological significance.

Overview of the Study

  • The researchers explored the reactions of heme proteins, specifically myoglobin derived from horse, with ligands such as carbon monoxide (CO) at different temperatures.
  • The focus was on transitioning from inhomogeneous (varying from point to point in a substance) to homogeneous (uniform) kinetics, both of which are states of protein-ligand reactions influenced by temperature.
  • The inhomogeneous reactions typically occur at cryogenic or extremely low temperatures, while homogeneous reactions are typical at room temperature. This study identified this transition at intermediate temperatures.

Tertiary Protein Relaxation Process

  • The observed transition was attributed to a tertiary protein relaxation process, which refers to changes in the overall protein shape.
  • In this process, the protein changes physical states, altering the energy barrier for the reaction, which the researchers describe as dynamically increasing in this context.

Methods and Findings

  • To confirm these observations, the research team used a blend of theoretical study and multipulse measurements, a technique used for temporal resolution of reaction kinetics.
  • The research findings validate that the transition in kinetics is not a static point but reflects the active fluctuation of the protein structure. This fluctuation is relevant in the biological context as it influences how the protein interacts with ligands like CO.

Biological Implications

  • The study suggests that this transition effect could have significant implications in the autocatalysis of the ligand release process, which is the self-acceleration of the discharging/releasing process of the ligand from the protein.
  • This can impact how various biochemical processes in the body are regulated and is especially relevant for mechanisms involving heme proteins such as myoglobin, which play crucial roles in oxygen transport and storage in muscle tissues.

Cite This Article

APA
Agmon N, Doster W, Post F. (1994). The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin. Biophys J, 66(5), 1612-1622. https://doi.org/10.1016/S0006-3495(94)80953-1

Publication

Biophysical journal
ISSN: 0006-3495
NlmUniqueID: 0370626
Country: United States
Language: English
Volume: 66
Issue: 5
Pages: 1612-1622

Researcher Affiliations

Agmon, N
  • Department of Physical Chemistry, Hebrew University, Jerusalem, Israel.
Doster, W
    Post, F

      MeSH Terms

      • Animals
      • Biophysical Phenomena
      • Biophysics
      • Carbon Monoxide / metabolism
      • Catalysis
      • Horses
      • In Vitro Techniques
      • Kinetics
      • Ligands
      • Models, Chemical
      • Myoglobin / chemistry
      • Myoglobin / metabolism
      • Protein Binding
      • Protein Conformation
      • Temperature
      • Thermodynamics

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      Citations

      This article has been cited 4 times.
      1. Samuni U, Dantsker D, Roche CJ, Friedman JM. Ligand recombination and a hierarchy of solvent slaved dynamics: the origin of kinetic phases in hemeproteins. Gene 2007 Aug 15;398(1-2):234-48.
        doi: 10.1016/j.gene.2007.04.032pubmed: 17570619google scholar: lookup
      2. Agmon N. Coupling of protein relaxation to ligand binding and migration in myoglobin. Biophys J 2004 Sep;87(3):1537-43.
        doi: 10.1529/biophysj.104.042929pubmed: 15345534google scholar: lookup
      3. McMahon BH, Müller JD, Wraight CA, Nienhaus GU. Electron transfer and protein dynamics in the photosynthetic reaction center. Biophys J 1998 May;74(5):2567-87.
        doi: 10.1016/S0006-3495(98)77964-0pubmed: 9591682google scholar: lookup
      4. Di Iorio EE, Tavernelli I, Yu W. Dynamic properties of monomeric insect erythrocruorin III from Chironomus thummi-thummi: relationships between structural flexibility and functional complexity. Biophys J 1997 Nov;73(5):2742-51.
        doi: 10.1016/S0006-3495(97)78303-6pubmed: 9370468google scholar: lookup
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