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

Horseradish peroxidase C

I Yamazaki, M Tamura, R Nakajima

    Molecular and Cellular Biochemistry
    |November 13, 1981
    PubMed
    Summary
    This summary is machine-generated.

    Horseradish peroxidase C (HRP) undergoes a two-step reduction, revealing redox-linked ionizations crucial for its enzymatic activity. Its structure and reactivity are further elucidated by comparing zinc-substituted HRP and NO-HRP complexes.

    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

    Molecular organization of bacteriochlorophyll in chlorosomes of the green photosynthetic bacteriumChloroflexus aurantiacus: Studies of fluorescence depolarization accompanied by energy transfer processes.

    Photosynthesis research·2013
    Same author

    Excitation energy transfer in the green photosynthetic bacterium Chloroflexus aurantiacus: A specific effect of 1-hexanol on the optical properties of baseplate and energy transfer processes.

    Photosynthesis research·2013
    Same author

    Identification of the starting point for spermatogenesis resumption in the post-diapause development of the sweet potato hornworm, Agrius convolvuli L.

    Journal of insect physiology·2011
    Same author

    Optically switching parallel processors by means of Langmuir-Blodgett multilayer films.

    Applied optics·2010
    Same author

    Applicability of a microchannel plate photo-multiplier to the time-correlated photon counting technique.

    Applied optics·2010
    Same author

    [Mitral valve papillary fibroelastoma; report of a case].

    Kyobu geka. The Japanese journal of thoracic surgery·2009
    Same journal

    PER1 reduces HIF-1α nuclear accumulation and modulates vascular remodeling in hepatocellular carcinoma.

    Molecular and cellular biochemistry·2026
    Same journal

    FCGR2A promoter variant reveals shared genetic susceptibility between IBD and stroke.

    Molecular and cellular biochemistry·2026
    Same journal

    Chlamydia psittaci induces GSDME-mediated pyroptosis via the ROS-JNK signaling pathway.

    Molecular and cellular biochemistry·2026
    Same journal

    Pentraxin 3 is an inflammation-related biomarker that distinguishes early-stage from mid-advanced cardiovascular-kidney-metabolic syndrome.

    Molecular and cellular biochemistry·2026
    Same journal

    High glucose-induced mitochondrial fission promotes Müller cell activation via suppression of the Hippo pathway.

    Molecular and cellular biochemistry·2026
    Same journal

    Correction to: Estradiol inhibits vascular endothelial cells pro-inflammatory activation induced by C-reactive protein.

    Molecular and cellular biochemistry·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Horseradish peroxidase C (HRP) is a key hemoprotein involved in various oxidative processes.
    • Understanding HRP's redox properties and reaction mechanisms is vital for its applications.

    Purpose of the Study:

    • To characterize the redox potentials and pH-dependent properties of HRP C.
    • To investigate the electronic structure of HRP intermediates, including Compound I.
    • To compare the coordination state of iron in HRP with other hemoproteins.

    Main Methods:

    • Redox titrations and potentiometric measurements to determine Eo' values.
    • Spectroscopic studies (flash photolysis) to probe coordination states.
    • Kinetic analysis of acid-alkaline transitions and substrate oxidation.

    Related Experiment Videos

    Main Results:

    • HRP C exhibits a two-step reduction with specific Eo' values and redox-linked ionizations at distinct pKa values.
    • Compound I of HRP contains a porphyrin pi-cation radical.
    • Zinc-substituted HRP C shows a different redox potential, indicating the role of the central metal ion.
    • Flash photolysis reveals pentacoordination of iron in HRP C, contrasting with hexacoordination in metmyoglobin.
    • Kinetic analysis provides rate constants for acid-alkaline conversions and substrate oxidation.

    Conclusions:

    • HRP C possesses complex redox behavior influenced by ionization states.
    • The porphyrin ring is significantly oxidized in Compound I.
    • Structural differences in metal coordination impact HRP's properties.
    • HRP C efficiently catalyzes substrate oxidation, forming reactive intermediates.