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

Asynchronous ligand binding and proton release in a root effect hemoglobin

W A Saffran, Q H Gibson

    The Journal of Biological Chemistry
    |May 10, 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

    The ratios of iron to oxygen, iron to colour and oxygen to colour in the blood of men and women.

    The Journal of physiology·2010
    Same author

    Familial idiopathic methaemoglobinaemia and its treatment with ascorbic acid.

    Clinical science·2010
    Same author

    Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity.

    Biochemistry·2001
    Same author

    Cavities and packing defects in the structural dynamics of myoglobin.

    EMBO reports·2001
    Same author

    Recombinational and mutagenic repair of psoralen interstrand cross-links in Saccharomyces cerevisiae.

    The Journal of biological chemistry·2001
    Same author

    Mapping the pathways for O2 entry into and exit from myoglobin.

    The Journal of biological chemistry·2000
    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

    Carbon monoxide (CO) binding to menhaden hemoglobin shows pH-dependent kinetics. Proton release lags CO binding, indicating a link between CO uptake and conformational changes in this Root effect hemoglobin.

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Physiological Chemistry

    Background:

    • Root effect hemoglobins exhibit unique oxygen binding properties, influenced by pH.
    • Understanding hemoglobin allosteric regulation is crucial for physiological function.
    • Menhaden (Brevoortia tyrannus) hemoglobin serves as a model for studying Root effect phenomena.

    Purpose of the Study:

    • To investigate the kinetics and equilibrium of carbon monoxide (CO) binding to menhaden hemoglobin.
    • To elucidate the allosteric regulation and proton release mechanisms associated with CO binding.
    • To analyze the pH dependence of CO binding and conformational changes in hemoglobin.

    Main Methods:

    • Flash photolysis and equilibrium measurements were employed to study CO binding kinetics and affinities.

    Related Experiment Videos

  • The two-state allosteric model, extended for chain differences, was used for data analysis.
  • Proton release kinetics were monitored using the pH indicator dye phenol red.

    • Main Results:

    • The allosteric constant (L) for CO binding varied significantly with pH, decreasing from 3 x 10(6) at pH 6.0 to 20 at pH 8.0.
    • Intrinsic rate constants for both the T and R states were found to be pH-dependent.
    • Proton release lagged behind CO binding, with longer lags observed at lower pH, suggesting a link to quaternary conformational changes.

    Conclusions:

    • CO binding to menhaden hemoglobin is a pH-sensitive process involving allosteric transitions.
    • Proton release is coupled to quaternary conformational changes during CO binding.
    • A modified two-state model incorporating pH-dependent intrinsic affinities best describes the observed proton release kinetics.