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(II) Schiff-base complexes and apoglobin stability.

J J Stephanos1, L M Jackson, A W Addison

  • 1Chemistry Department, Faculty of Science, El-Menoufia University, Shebin El-Kom, Egypt.

Journal of Inorganic Biochemistry
|May 20, 1999
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

medna-metadata: an open-source data management system for tracking environmental DNA samples and metadata.

Bioinformatics (Oxford, England)·2022
Same author

Pandemic H1N1 Influenza Infection and Vaccination in Humans Induces Cross-Protective Antibodies that Target the Hemagglutinin Stem.

Frontiers in immunology·2012
Same author

Preparation and characterization of chitosan-grafted-poly(2-amino-4,5-pentamethylene-thiophene-3-carboxylic acid N'-acryloyl-hydrazide) chelating resin for removal of Cu(II), Co(II) and Ni(II) metal ions from aqueous solutions.

International journal of biological macromolecules·2011
Same author

Novel concepts about normal sexual differentiation of reproductive neuroendocrine function and the developmental origins of female reproductive dysfunction: the sheep model.

Society of Reproduction and Fertility supplement·2007
Same author

Gastrointestinal effects of COX-2 inhibitors.

Expert opinion on investigational drugs·2005
Same author

NSAIDs and the GI tract-potential hazards and benefits.

Apoptosis : an international journal on programmed cell death·2003

N,N'-Propylene-bis-(N-salicylidene)copper(II) (Cu(Salprn)) stabilizes apomyoglobin, influencing its optical and ESR spectra. This copper(II) Schiff-base complex facilitates hemin extraction from hemoglobin, with a mechanism involving dissociative and associative pathways.

Area of Science:

  • Biochemistry
  • Coordination Chemistry
  • Spectroscopy

Background:

  • Apomyoglobin's structure and function are critical in biological systems.
  • Copper(II) Schiff-base complexes offer unique coordination properties.
  • Understanding protein-ligand interactions is key to biomimetic chemistry.

Purpose of the Study:

  • To investigate the stabilization of apomyoglobin by N,N '-Propylene-bis-(N-salicylidene)copper(II) (Cu(Salprn)).
  • To analyze the spectral properties and coordination environment of the Cu(Salprn)-apomyoglobin complex.
  • To determine the effect of this complex on hemin extraction from Glycera dibranchiata hemoglobin.

Main Methods:

  • UV-Vis spectroscopy to study electronic transitions.
  • Electron Spin Resonance (ESR) spectroscopy to probe the copper coordination sphere.

Related Experiment Videos

  • Kinetic analysis of hemin extraction by the modified apomyoglobin.

    • Main Results:

    • Cu(Salprn) stabilizes apomyoglobin, with spectral shifts possibly due to solvatochromism or ligand binding.
    • ESR data indicate no alteration in the copper's first coordination sphere.
    • Apomyoglobin complexed with Cu(Salprn) retains its ability to extract hemin, with rate constants evaluated.

    Conclusions:

    • Cu(Salprn) is an effective stabilizer for apomyoglobin.
    • The copper center's coordination environment remains largely unchanged.
    • The complex participates in a complex hemin transfer mechanism with dissociative and associative pathways.