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

Copper(I) . bleomycin. A structurally unique oxidation-reduction active complex.

N J Oppenheimer, C Chang, L O Rodriguez

    The Journal of Biological Chemistry
    |February 25, 1981
    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

    A pulsed-field ionization photoelectron secondary ion coincidence study of the H2+ (X,upsilon+=0-15,N+=1)+He proton transfer reaction.

    The Journal of chemical physics·2005
    Same author

    Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure.

    Biochemistry·2005
    Same author

    [Determination of beryllium in geological samples with slurry sampling and probe atomization in graphite furnace atomic absorption spectrometry].

    Guang pu xue yu guang pu fen xi = Guang pu·2005
    Same author

    Vibration-assisted electron tunneling in C140 transistors.

    Nano letters·2005
    Same author

    Extraperitoneal laparoscopic pyeloplasty for primary and secondary ureteropelvic junction obstruction.

    The Journal of urology·2004
    Same author

    The androgen receptor in spermatogenesis.

    Cytogenetic and genome research·2004
    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

    Copper(I) and Copper(II) form stable complexes with bleomycin (BLM), showing higher affinity than iron. The unique geometry of copper(I) bleomycin complexes is crucial for understanding bleomycin

    Area of Science:

    • Biochemistry
    • Medicinal Chemistry
    • Molecular Biology

    Background:

    • Bleomycin (BLM) is a potent anti-cancer drug that functions by interacting with DNA.
    • The metal-binding properties of bleomycin are critical for its biological activity, with iron (Fe) being extensively studied.
    • Understanding how other metal ions, such as copper (Cu), interact with bleomycin is essential for exploring new therapeutic strategies.

    Purpose of the Study:

    • To investigate the complexation of copper(I) and copper(II) with bleomycin.
    • To compare the DNA-binding affinity of copper-bleomycin complexes with iron-bleomycin complexes.
    • To elucidate the coordination geometry of copper(I)-bleomycin complexes and its implications for bleomycin's activity.

    Main Methods:

    • Potentiometric titration to determine metal-ligand binding affinities.

    Related Experiment Videos

  • 1H Nuclear Magnetic Resonance (NMR) spectroscopy to analyze complex structures.
  • DNA-induced fluorescence quenching assays to assess DNA-binding interactions.
  • Main Results:

    • Both Cu(I) and Cu(II) form stable 1:1 complexes with bleomycin, exhibiting higher affinity than Fe(II).
    • Cu(I)-bleomycin complexes bind to DNA with an affinity comparable to Fe(II)-bleomycin.
    • 1H NMR and potentiometric titration data reveal distinct geometries for Cu(I)-bleomycin complexes compared to other studied metal-bleomycin complexes.

    Conclusions:

    • Copper ions bind to bleomycin with high affinity, influencing its DNA interaction capabilities.
    • The unique coordination geometry of Cu(I)-bleomycin complexes is a key factor in its redox activity and potential biological function.
    • These findings provide structural insights into bleomycin's mechanism of action and suggest potential for copper-based drug development.