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Related Experiment Videos

A structure of pyridine nucleotides in solution.

N J Oppenheimer, L J Arnold, N O Kaplan

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1971
    PubMed
    Summary

    Nuclear magnetic resonance reveals pyridine coenzymes primarily adopt a folded structure in solution. This conformation, observed in both oxidized and reduced forms, suggests significant structural similarity between these states.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Molecular Biophysics

    Background:

    • Pyridine coenzymes, such as NAD+ and NADH, are essential biological redox carriers.
    • Understanding their solution structure is crucial for elucidating their catalytic mechanisms.
    • Previous structural studies have yielded varying interpretations of coenzyme conformations.

    Purpose of the Study:

    • To re-examine the solution structure of pyridine coenzymes using advanced NMR spectroscopy.
    • To investigate conformational changes upon reduction of the pyridine ring.
    • To present a structural model for the folded conformation of pyridine coenzymes.

    Main Methods:

    • High-frequency (220-MHz) nuclear magnetic resonance (NMR) spectroscopy was employed.
    • Structural analysis focused on proton resonances of the coenzyme molecules in solution.
    • Comparison of spectral data for oxidized and reduced forms of DPN+ and its analogs.

    Main Results:

    • A predominant folded structure was identified in rapid equilibrium with an open form.
    • Reduced pyridine coenzymes predominantly exhibit folding of the dihydropyridine ring against the adenine moiety.
    • Oxidized coenzymes appear to adopt the same folded structure.
    • Minimal conformational changes were observed in ribose protons upon pyridine ring reduction.

    Conclusions:

    • Pyridine coenzymes exist primarily in a specific folded conformation in solution.
    • The folded structure is conserved between oxidized and reduced states, indicating high structural similarity.
    • A structural model for the folded conformation of pyridine coenzymes has been proposed based on NMR data.

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