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

Cytochrome c1 complexes.

Y L Chiang, T E King

    The Journal of Biological Chemistry
    |March 25, 1979
    PubMed
    Summary
    This summary is machine-generated.

    Cytochrome c1 forms complexes with cytochrome c and oxidase, including a stable 1:1 c1-oxidase complex and a 1:1:1 ternary complex. These interactions involve protein-protein binding and alter cytochrome c1 aggregation states.

    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

    Human Phenotypic Diversity: An Evolutionary Perspective.

    Current topics in developmental biology·2016
    Same author

    Bronchoalveolar lavage pepsin in acute exacerbation of idiopathic pulmonary fibrosis.

    The European respiratory journal·2011
    Same author

    Fatigue in sarcoidosis: American versus Dutch patients.

    Sarcoidosis, vasculitis, and diffuse lung diseases : official journal of WASOG·2010
    Same author

    Usual interstitial pneumonia in rheumatoid arthritis-associated interstitial lung disease.

    The European respiratory journal·2009
    Same author

    Quality of life and dyspnoea in patients treated with bosentan for idiopathic pulmonary fibrosis (BUILD-1).

    The European respiratory journal·2009
    Same author

    Idiopathic pulmonary fibrosis and nonspecific interstitial pneumonia should stay separate.

    The European respiratory journal·2008
    Same journal

    Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

    The Journal of biological chemistry·2026
    Same journal

    Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

    The Journal of biological chemistry·2026
    Same journal

    Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

    The Journal of biological chemistry·2026
    Same journal

    Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

    The Journal of biological chemistry·2026
    Same journal

    YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

    The Journal of biological chemistry·2026
    Same journal

    ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

    The Journal of biological chemistry·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein-Protein Interactions

    Background:

    • Cytochrome c1 is known to form an active complex with cytochrome c.
    • Understanding the interactions of cytochrome c1 with other respiratory chain components is crucial for elucidating electron transport mechanisms.

    Purpose of the Study:

    • To investigate the complex formation of cytochrome c1 with cytochrome c and cytochrome oxidase.
    • To characterize the properties and stability of these complexes.
    • To explore the role of protein-protein interactions in the assembly of respiratory complexes.

    Main Methods:

    • Ammonium sulfate fractionation for purification of the cytochrome c1-oxidase complex.
    • Spectrophotometry and circular dichroism for characterization.

    Related Experiment Videos

  • Sedimentation analysis to determine complex formation and aggregation states.
  • Incorporation into phospholipid vesicles.

    • Main Results:

    • Cytochrome c1 forms a stable 1:1 complex with cytochrome oxidase, stable in high ionic strength and neutral pH.
    • Purified cytochrome c1 aggregates, but within the c1-oxidase complex, it appears depolymerized.
    • A ternary complex of cytochrome c1, cytochrome c, and oxidase (1:1:1 ratio) can be formed through various combinations of pre-formed complexes or individual components.
    • Cytochrome c1 can be incorporated into phospholipid vesicles.

    Conclusions:

    • Cytochrome c1 participates in multiple protein-protein interactions within the electron transport chain.
    • The formation of c1-oxidase and ternary complexes is driven by protein-protein interactions.
    • Complex formation influences the aggregation state of cytochrome c1.