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

The coordinating properties of d-biotin

H Sigel

    Experientia
    |January 1, 1981
    PubMed
    Summary

    d-biotin, a coenzyme, has three potential metal ion binding sites: carboxylate, ureido, and thioether sulfur. These sites, along with hydrogen bonding and hydrophobic interactions, facilitate enzyme-substrate complex formation.

    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

    Direct current combined with x-ray therapy; erythema studies; preliminary experiments.

    The Journal of investigative dermatology·2010
    Same author

    Metal ions in biological systems, volume 35: iron transport and storage microorganisms, plants, and animals.

    Metal-based drugs·2008
    Same author

    Metal ion-binding properties of the diphosphate ester analogue, methylphosphonylphosphate, in aqueous solution.

    Metal-based drugs·2008
    Same author

    Ternary Copper(II) Complexes in Solution Formed With 8-Aza Derivatives of the Antiviral Nucleotide Analogue 9-[2-(Phosphonomethoxy)Ethyl]Adenine (PMEA).

    Metal-based drugs·2008
    Same author

    The self-association of flavin mononucleotide (FMN(2-)) as determined by (1)H NMR shift measurements.

    Biophysical chemistry·2006
    Same author

    [Myocardial infarction and coronary artery ventricular fistulas due to blunt chest trauma]

    Deutsche medizinische Wochenschrift (1946)·2003

    Area of Science:

    • Biochemistry
    • Bioinorganic Chemistry

    Background:

    • d-biotin is a vital coenzyme involved in numerous metabolic processes.
    • Understanding biotin's coordination chemistry is crucial for elucidating enzyme mechanisms.

    Purpose of the Study:

    • To investigate the metal ion binding properties of d-biotin.
    • To explore the role of different functional groups in biotin's interactions with metal ions and proteins.

    Main Methods:

    • Comparative analysis of the coordinating properties of biotin's functional groups.
    • Identification of potential hydrogen bonding and hydrophobic interactions.

    Main Results:

    • d-biotin exhibits three primary metal ion binding sites: carboxylate, ureido, and thioether sulfur.
    • Hydrogen bonding involving the ureido group may be significant for biotin-bicarbonate recognition.
    • Hydrophobic interactions of the valerate side chain contribute to protein binding.

    Conclusions:

    • The specific coordination and interaction modes of d-biotin are essential for its biological function.
    • Stereoselective sulfur-metal ion coordination and hydrophobic interactions enable the precise "fixation" of biotinyl moieties.
    • These interactions are critical for forming active enzyme-substrate complexes.

    Related Experiment Videos