Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Interaction between cytochrome c and cytochrome b5.

J Stonehuerner, J B Williams, F Millett

    Biochemistry
    |November 27, 1979
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Probing Instantaneous Single-Molecule Chirality in the Planar Ground State of Formic Acid.

    Physical review letters·2026
    Same author

    Enantioselective One-Photon Excitation of Formic Acid.

    Physical review letters·2024
    Same author

    Tracking ultrafast non-adiabatic dissociation dynamics of the deuterated water dication molecule.

    The Journal of chemical physics·2024
    Same author

    Efficiency of charge transfer in changing the dissociation dynamics of OD+ transients formed after the photo-fragmentation of D2O.

    The Journal of chemical physics·2023
    Same author

    Atomic autoionization in the photo-dissociation of super-excited deuterated water molecules fragmenting into D<sup>+</sup> + O<sup>+</sup> + D.

    Physical chemistry chemical physics : PCCP·2023
    Same author

    High-energy molecular-frame photoelectron angular distributions: a molecular bond-length ruler.

    Physical chemistry chemical physics : PCCP·2023

    The study reveals that electrostatic interactions, specifically five to seven complementary charge interactions between lysine and carboxyl groups, govern the reduction of cytochrome c by cytochrome b5. These proteins form a stable complex at low ionic strength.

    Area of Science:

    • Biochemistry
    • Protein-protein interactions
    • Electron transfer reactions

    Background:

    • Cytochrome c and cytochrome b5 are key electron transfer proteins.
    • Understanding their interaction mechanism is crucial for elucidating cellular redox processes.

    Purpose of the Study:

    • To investigate the role of electrostatic interactions in the reduction of cytochrome c by cytochrome b5.
    • To quantify the nature and extent of these interactions.

    Main Methods:

    • Studied reaction kinetics across a wide range of ionic strengths using four buffer systems.
    • Employed ultracentrifugation and gel permeation chromatography to assess complex formation.

    Main Results:

    • Reaction rate showed a linear decrease with increasing ionic strength (I1/2), indicating significant electrostatic contributions.

    Related Experiment Videos

  • Quantitative agreement with Wherland & Gray theory was achieved with an effective interaction radius of 2 Å.
  • Calculated five to seven complementary charge interactions between specific residues (lysine on cytochrome c, carboxyl on cytochrome b5).
  • Demonstrated stable complex formation between cytochrome b5 and cytochrome c at low ionic strength.

    • Conclusions:

    • The interaction between cytochrome c and cytochrome b5 is dominated by specific electrostatic interactions.
    • A model involving 5-7 complementary charge pairs accurately describes the protein-protein binding.
    • Protein complex formation is dependent on ionic strength, favoring association at lower concentrations.